The oxygen-carrying proteins of ERYTHROCYTES. They are found in all vertebrates and some invertebrates. The number of globin subunits in the hemoglobin quaternary structure differs between species. Structures range from monomeric to a variety of multimeric arrangements.
Normal adult human hemoglobin. The globin moiety consists of two alpha and two beta chains.
Hemoglobins characterized by structural alterations within the molecule. The alteration can be either absence, addition or substitution of one or more amino acids in the globin part of the molecule at selected positions in the polypeptide chains.
The major component of hemoglobin in the fetus. This HEMOGLOBIN has two alpha and two gamma polypeptide subunits in comparison to normal adult hemoglobin, which has two alpha and two beta polypeptide subunits. Fetal hemoglobin concentrations can be elevated (usually above 0.5%) in children and adults affected by LEUKEMIA and several types of ANEMIA.
An abnormal hemoglobin resulting from the substitution of valine for glutamic acid at position 6 of the beta chain of the globin moiety. The heterozygous state results in sickle cell trait, the homozygous in sickle cell anemia.
A commonly occurring abnormal hemoglobin in which lysine replaces a glutamic acid residue at the sixth position of the beta chains. It results in reduced plasticity of erythrocytes.
A compound formed by the combination of hemoglobin and oxygen. It is a complex in which the oxygen is bound directly to the iron without causing a change from the ferrous to the ferric state.
Minor hemoglobin components of human erythrocytes designated A1a, A1b, and A1c. Hemoglobin A1c is most important since its sugar moiety is glucose covalently bound to the terminal amino acid of the beta chain. Since normal glycohemoglobin concentrations exclude marked blood glucose fluctuations over the preceding three to four weeks, the concentration of glycosylated hemoglobin A is a more reliable index of the blood sugar average over a long period of time.
An abnormal hemoglobin that results from the substitution of lysine for glutamic acid at position 26 of the beta chain. It is most frequently observed in southeast Asian populations.
An adult hemoglobin component normally present in hemolysates from human erythrocytes in concentrations of about 3%. The hemoglobin is composed of two alpha chains and two delta chains. The percentage of HbA2 varies in some hematologic disorders, but is about double in beta-thalassemia.
Methemoglobin is a form of hemoglobin where the iron within the heme group is in the ferric (Fe3+) state, unable to bind oxygen and leading to impaired oxygen-carrying capacity of the blood.
A family of hemoglobin-like proteins found in BACTERIA; PLANTS; and unicellular eukaryotes. Truncated hemoglobins are distantly related to vertebrate hemoglobins and are typically shorter than vertebrate hemoglobins by 20-40 residues.
A reduction in the number of circulating ERYTHROCYTES or in the quantity of HEMOGLOBIN.
A group of inherited disorders characterized by structural alterations within the hemoglobin molecule.
Carboxyhemoglobin is a form of hemoglobin in which the heme group is chemically bonded to carbon monoxide, reducing its ability to transport oxygen and leading to toxic effects when present in high concentrations.
Measurement of hemoglobin concentration in blood.
An element with atomic symbol O, atomic number 8, and atomic weight [15.99903; 15.99977]. It is the most abundant element on earth and essential for respiration.
A disease characterized by compensated hemolysis with a normal hemoglobin level or a mild to moderate anemia. There may be intermittent abdominal discomfort, splenomegaly, and slight jaundice.
Substances that are used in place of blood, for example, as an alternative to BLOOD TRANSFUSIONS after blood loss to restore BLOOD VOLUME and oxygen-carrying capacity to the blood circulation, or to perfuse isolated organs.
A group of abnormal hemoglobins with similar electrophoretic characteristics. They have faster electrophoretic mobility and different amino acid substitutions in either the alpha or beta chains than normal adult hemoglobin. Some of the variants produce hematologic abnormalities, others result in no clinical disorders.
An abnormal hemoglobin composed of four beta chains. It is caused by the reduced synthesis of the alpha chain. This abnormality results in ALPHA-THALASSEMIA.
2,3-Diphosphoglycerate (2,3-DPG) is a physiological modulator of hemoglobin oxygen affinity, reducing its attraction to oxygen in red blood cells, which facilitates the release of oxygen to tissues with lower oxygen concentrations.
A disease characterized by chronic hemolytic anemia, episodic painful crises, and pathologic involvement of many organs. It is the clinical expression of homozygosity for hemoglobin S.
Red blood cells. Mature erythrocytes are non-nucleated, biconcave disks containing HEMOGLOBIN whose function is to transport OXYGEN.
A highly anionic organic phosphate which is present in human red blood cells at about the same molar ratio as hemoglobin. It binds to deoxyhemoglobin but not the oxygenated form, therefore diminishing the oxygen affinity of hemoglobin. This is essential in enabling hemoglobin to unload oxygen in tissue capillaries. It is also an intermediate in the conversion of 3-phosphoglycerate to 2-phosphoglycerate by phosphoglycerate mutase (EC 5.4.2.1). (From Stryer Biochemistry, 4th ed, p160; Enzyme Nomenclature, 1992, p508)
A superfamily of proteins containing the globin fold which is composed of 6-8 alpha helices arranged in a characterstic HEME enclosing structure.
The color-furnishing portion of hemoglobin. It is found free in tissues and as the prosthetic group in many hemeproteins.
A group of hereditary hemolytic anemias in which there is decreased synthesis of one or more hemoglobin polypeptide chains. There are several genetic types with clinical pictures ranging from barely detectable hematologic abnormality to severe and fatal anemia.
A metallic element with atomic symbol Fe, atomic number 26, and atomic weight 55.85. It is an essential constituent of HEMOGLOBINS; CYTOCHROMES; and IRON-BINDING PROTEINS. It plays a role in cellular redox reactions and in the transport of OXYGEN.
The volume of packed RED BLOOD CELLS in a blood specimen. The volume is measured by centrifugation in a tube with graduated markings, or with automated blood cell counters. It is an indicator of erythrocyte status in disease. For example, ANEMIA shows a low value; POLYCYTHEMIA, a high value.
Glycoprotein hormone, secreted chiefly by the KIDNEY in the adult and the LIVER in the FETUS, that acts on erythroid stem cells of the BONE MARROW to stimulate proliferation and differentiation.
One of the sickle cell disorders characterized by the presence of both hemoglobin S and hemoglobin C. It is similar to, but less severe than sickle cell anemia.
Carbon monoxide (CO). A poisonous colorless, odorless, tasteless gas. It combines with hemoglobin to form carboxyhemoglobin, which has no oxygen carrying capacity. The resultant oxygen deprivation causes headache, dizziness, decreased pulse and respiratory rates, unconsciousness, and death. (From Merck Index, 11th ed)
Agents which improve the quality of the blood, increasing the hemoglobin level and the number of erythrocytes. They are used in the treatment of anemias.
The number of RED BLOOD CELLS per unit volume in a sample of venous BLOOD.
ERYTHROCYTE size and HEMOGLOBIN content or concentration, usually derived from ERYTHROCYTE COUNT; BLOOD hemoglobin concentration; and HEMATOCRIT. The indices include the mean corpuscular volume (MCV), the mean corpuscular hemoglobin (MCH), and the mean corpuscular hemoglobin concentration (MCHC).
Anemia characterized by decreased or absent iron stores, low serum iron concentration, low transferrin saturation, and low hemoglobin concentration or hematocrit value. The erythrocytes are hypochromic and microcytic and the iron binding capacity is increased.
Complexing agent for removal of traces of heavy metal ions. It acts also as a hypocalcemic agent.
Plasma glycoproteins that form a stable complex with hemoglobin to aid the recycling of heme iron. They are encoded in man by a gene on the short arm of chromosome 16.
Electrophoresis applied to BLOOD PROTEINS.
A disorder characterized by reduced synthesis of the beta chains of hemoglobin. There is retardation of hemoglobin A synthesis in the heterozygous form (thalassemia minor), which is asymptomatic, while in the homozygous form (thalassemia major, Cooley's anemia, Mediterranean anemia, erythroblastic anemia), which can result in severe complications and even death, hemoglobin A synthesis is absent.
The condition of being heterozygous for hemoglobin S.
A group of abnormal hemoglobins in which amino acid substitutions take place in either the alpha or beta chains but near the heme iron. This results in facilitated oxidation of the hemoglobin to yield excess methemoglobin which leads to cyanosis.
Agents used to prevent or reverse the pathological events leading to sickling of erythrocytes in sickle cell conditions.
A disorder characterized by reduced synthesis of the alpha chains of hemoglobin. The severity of this condition can vary from mild anemia to death, depending on the number of genes deleted.
Iron-containing proteins that are widely distributed in animals, plants, and microorganisms. Their major function is to store IRON in a nontoxic bioavailable form. Each ferritin molecule consists of ferric iron in a hollow protein shell (APOFERRITINS) made of 24 subunits of various sequences depending on the species and tissue types.
Members of the alpha-globin family. In humans, they are encoded in a gene cluster on CHROMOSOME 16. They include zeta-globin and alpha-globin. There are also pseudogenes of zeta (theta-zeta) and alpha (theta-alpha) in the cluster. Adult HEMOGLOBIN is comprised of 2 alpha-globin chains and 2 beta-globin chains.
Oxygen-carrying RED BLOOD CELLS in mammalian blood that are abnormal in structure or function.
A conjugated protein which is the oxygen-transporting pigment of muscle. It is made up of one globin polypeptide chain and one heme group.
The destruction of ERYTHROCYTES by many different causal agents such as antibodies, bacteria, chemicals, temperature, and changes in tonicity.
Members of the beta-globin family. In humans, they are encoded in a gene cluster on CHROMOSOME 11. They include epsilon-globin, gamma-globin, delta-globin and beta-globin. There is also a pseudogene of beta (theta-beta) in the gene cluster. Adult HEMOGLOBIN is comprised of two ALPHA-GLOBIN chains and two beta-globin chains.
The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)
Anemia characterized by a decrease in the ratio of the weight of hemoglobin to the volume of the erythrocyte, i.e., the mean corpuscular hemoglobin concentration is less than normal. The individual cells contain less hemoglobin than they could have under optimal conditions. Hypochromic anemia may be caused by iron deficiency from a low iron intake, diminished iron absorption, or excessive iron loss. It can also be caused by infections or other diseases, therapeutic drugs, lead poisoning, and other conditions. (Stedman, 25th ed; from Miale, Laboratory Medicine: Hematology, 6th ed, p393)
The production of red blood cells (ERYTHROCYTES). In humans, erythrocytes are produced by the YOLK SAC in the first trimester; by the liver in the second trimester; by the BONE MARROW in the third trimester and after birth. In normal individuals, the erythrocyte count in the peripheral blood remains relatively constant implying a balance between the rate of erythrocyte production and rate of destruction.
The presence of free HEMOGLOBIN in the URINE, indicating hemolysis of ERYTHROCYTES within the vascular system. After saturating the hemoglobin-binding proteins (HAPTOGLOBINS), free hemoglobin begins to appear in the urine.
An increase in the total red cell mass of the blood. (Dorland, 27th ed)
Chloro(7,12-diethenyl-3,8,13,17-tetramethyl-21H,23H-porphine-2,18-dipropanoato(4-)-N(21),N(22),N(23),N(24)) ferrate(2-) dihydrogen.
The art or process of comparing photometrically the relative intensities of the light in different parts of the spectrum.
Electrophoresis in which cellulose acetate is the diffusion medium.
The co-occurrence of pregnancy and a blood disease (HEMATOLOGIC DISEASES) which involves BLOOD CELLS or COAGULATION FACTORS. The hematologic disease may precede or follow FERTILIZATION and it may or may not have a deleterious effect on the pregnant woman or FETUS.
Abnormal intracellular inclusions, composed of denatured hemoglobin, found on the membrane of red blood cells. They are seen in thalassemias, enzymopathies, hemoglobinopathies, and after splenectomy.
Repetitive withdrawal of small amounts of blood and replacement with donor blood until a large proportion of the blood volume has been exchanged. Used in treatment of fetal erythroblastosis, hepatic coma, sickle cell anemia, disseminated intravascular coagulation, septicemia, burns, thrombotic thrombopenic purpura, and fulminant malaria.
Tests used in the analysis of the hemic system.
A phylum of metazoan invertebrates comprising the segmented worms, and including marine annelids (POLYCHAETA), freshwater annelids, earthworms (OLIGOCHAETA), and LEECHES. Only the leeches are of medical interest. (Dorland, 27th ed)
The rate dynamics in chemical or physical systems.
The number of RETICULOCYTES per unit volume of BLOOD. The values are expressed as a percentage of the ERYTHROCYTE COUNT or in the form of an index ("corrected reticulocyte index"), which attempts to account for the number of circulating erythrocytes.
A class of annelid worms with few setae per segment. It includes the earthworms such as Lumbricus and Eisenia.
Proteins that contain an iron-porphyrin, or heme, prosthetic group resembling that of hemoglobin. (From Lehninger, Principles of Biochemistry, 1982, p480)
Glucose in blood.
The introduction of whole blood or blood component directly into the blood stream. (Dorland, 27th ed)
Stable iron atoms that have the same atomic number as the element iron, but differ in atomic weight. Fe-54, 57, and 58 are stable iron isotopes.
A heterogeneous group of disorders characterized by HYPERGLYCEMIA and GLUCOSE INTOLERANCE.
A noninvasive technique that uses the differential absorption properties of hemoglobin and myoglobin to evaluate tissue oxygenation and indirectly can measure regional hemodynamics and blood flow. Near-infrared light (NIR) can propagate through tissues and at particular wavelengths is differentially absorbed by oxygenated vs. deoxygenated forms of hemoglobin and myoglobin. Illumination of intact tissue with NIR allows qualitative assessment of changes in the tissue concentration of these molecules. The analysis is also used to determine body composition.
Immature ERYTHROCYTES. In humans, these are ERYTHROID CELLS that have just undergone extrusion of their CELL NUCLEUS. They still contain some organelles that gradually decrease in number as the cells mature. RIBOSOMES are last to disappear. Certain staining techniques cause components of the ribosomes to precipitate into characteristic "reticulum" (not the same as the ENDOPLASMIC RETICULUM), hence the name reticulocytes.
A subclass of DIABETES MELLITUS that is not INSULIN-responsive or dependent (NIDDM). It is characterized initially by INSULIN RESISTANCE and HYPERINSULINEMIA; and eventually by GLUCOSE INTOLERANCE; HYPERGLYCEMIA; and overt diabetes. Type II diabetes mellitus is no longer considered a disease exclusively found in adults. Patients seldom develop KETOSIS but often exhibit OBESITY.
An amino sugar formed when glucose non-enzymatically reacts with the N-terminal amino group of proteins. The fructose moiety is derived from glucose by the "classical" Amadori rearrangement.
Electrophoresis in which a starch gel (a mixture of amylose and amylopectin) is used as the diffusion medium.
A condition of inadequate circulating red blood cells (ANEMIA) or insufficient HEMOGLOBIN due to premature destruction of red blood cells (ERYTHROCYTES).
Electrophoresis in which a pH gradient is established in a gel medium and proteins migrate until they reach the site (or focus) at which the pH is equal to their isoelectric point.
The PROTEIN SUBUNITS that comprise multimeric HEMOGLOBINS.
Chemical bond cleavage reactions resulting from absorption of radiant energy.
Compounds and molecular complexes that consist of very large numbers of atoms and are generally over 500 kDa in size. In biological systems macromolecular substances usually can be visualized using ELECTRON MICROSCOPY and are distinguished from ORGANELLES by the lack of a membrane structure.
The number of LEUKOCYTES and ERYTHROCYTES per unit volume in a sample of venous BLOOD. A complete blood count (CBC) also includes measurement of the HEMOGLOBIN; HEMATOCRIT; and ERYTHROCYTE INDICES.
The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).
Elements of limited time intervals, contributing to particular results or situations.
The transfer of erythrocytes from a donor to a recipient or reinfusion to the donor.
The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.
Inorganic or organic compounds that contain divalent iron.
The modification of the reactivity of ENZYMES by the binding of effectors to sites (ALLOSTERIC SITES) on the enzymes other than the substrate BINDING SITES.
Therapy for the insufficient cleansing of the BLOOD by the kidneys based on dialysis and including hemodialysis, PERITONEAL DIALYSIS, and HEMODIAFILTRATION.
Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.
A genus of gram-negative, aerobic or microaerophilic, colorless filaments. It is nonfruiting, motile by gliding, and found in freshwater sediments and cow dung. One species (V. stercoraria) is considered morphologically to be a streptobacillus. That species is strictly aerobic and produces a homodimeric bacterial hemoglobin, especially under oxygen-limited growth conditions. (From Bergey's Manual of Determinative Bacteriology, 9th ed)
Volume of circulating ERYTHROCYTES . It is usually measured by RADIOISOTOPE DILUTION TECHNIQUE.
The senescence of RED BLOOD CELLS. Lacking the organelles that make protein synthesis possible, the mature erythrocyte is incapable of self-repair, reproduction, and carrying out certain functions performed by other cells. This limits the average life span of an erythrocyte to 120 days.
The pressure that would be exerted by one component of a mixture of gases if it were present alone in a container. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)
A class of marine annelids including sandworms, tube worms, clamworms, and fire worms. It includes also the genus Myxicola infundibulum.
Reduction of blood viscosity usually by the addition of cell free solutions. Used clinically (1) in states of impaired microcirculation, (2) for replacement of intraoperative blood loss without homologous blood transfusion, and (3) in cardiopulmonary bypass and hypothermia.
A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471).
A class in the phylum MOLLUSCA comprised of mussels; clams; OYSTERS; COCKLES; and SCALLOPS. They are characterized by a bilaterally symmetrical hinged shell and a muscular foot used for burrowing and anchoring.
Proteins prepared by recombinant DNA technology.
A clinical manifestation consisting of an unnatural paleness of the skin.
A family of nonbiting midges, in the order DIPTERA. Salivary glands of the genus Chironomus are used in studies of cellular genetics and biochemistry.
Members of the beta-globin family. In humans, two non-allelic types of gamma-globin - A gamma and G gamma are encoded in the beta-globin gene cluster on CHROMOSOME 11. Two gamma-globin chains combine with two ZETA-GLOBIN chains to form the embryonic hemoglobin Portland. Fetal HEMOGLOBIN F is formed from two gamma-globin chains combined with two ALPHA-GLOBIN chains.
The determination of oxygen-hemoglobin saturation of blood either by withdrawing a sample and passing it through a classical photoelectric oximeter or by electrodes attached to some translucent part of the body like finger, earlobe, or skin fold. It includes non-invasive oxygen monitoring by pulse oximetry.
Diazo derivatives of aniline, used as a reagent for sugars, ketones, and aldehydes. (Dorland, 28th ed)
Sulfhemoglobin is a dark methemoglobin derivative formed by the reaction of hemoglobin with sulfide or certain drugs, characterized by its chocolate-brown color and decreased oxygen-carrying capacity.
The end-stage of CHRONIC RENAL INSUFFICIENCY. It is characterized by the severe irreversible kidney damage (as measured by the level of PROTEINURIA) and the reduction in GLOMERULAR FILTRATION RATE to less than 15 ml per min (Kidney Foundation: Kidney Disease Outcome Quality Initiative, 2002). These patients generally require HEMODIALYSIS or KIDNEY TRANSPLANTATION.
A free radical gas produced endogenously by a variety of mammalian cells, synthesized from ARGININE by NITRIC OXIDE SYNTHASE. Nitric oxide is one of the ENDOTHELIUM-DEPENDENT RELAXING FACTORS released by the vascular endothelium and mediates VASODILATION. It also inhibits platelet aggregation, induces disaggregation of aggregated platelets, and inhibits platelet adhesion to the vascular endothelium. Nitric oxide activates cytosolic GUANYLATE CYCLASE and thus elevates intracellular levels of CYCLIC GMP.
An antineoplastic agent that inhibits DNA synthesis through the inhibition of ribonucleoside diphosphate reductase.
Iron or iron compounds used in foods or as food. Dietary iron is important in oxygen transport and the synthesis of the iron-porphyrin proteins hemoglobin, myoglobin, cytochromes, and cytochrome oxidase. Insufficient amounts of dietary iron can lead to iron-deficiency anemia.
Porphyrins with four methyl, two vinyl, and two propionic acid side chains attached to the pyrrole rings. Protoporphyrin IX occurs in hemoglobin, myoglobin, and most of the cytochromes.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
Analysis of the intensity of Raman scattering of monochromatic light as a function of frequency of the scattered light.
An examination of chemicals in the blood.
The semi-permeable outer structure of a red blood cell. It is known as a red cell 'ghost' after HEMOLYSIS.
High molecular weight (1,500,000 to 3,000,000) hemoglobins found in the plasma of many polychete and oligochete annelid worms and various mollusks. They bind one mole of oxygen per heme and function as oxygen carriers.
Evaluation undertaken to assess the results or consequences of management and procedures used in combating disease in order to determine the efficacy, effectiveness, safety, and practicability of these interventions in individual cases or series.
The measurement of the amplitude of the components of a complex waveform throughout the frequency range of the waveform. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)
Mercury-containing benzoic acid derivatives.
Observation of a population for a sufficient number of persons over a sufficient number of years to generate incidence or mortality rates subsequent to the selection of the study group.
Measurable and quantifiable biological parameters (e.g., specific enzyme concentration, specific hormone concentration, specific gene phenotype distribution in a population, presence of biological substances) which serve as indices for health- and physiology-related assessments, such as disease risk, psychiatric disorders, environmental exposure and its effects, disease diagnosis, metabolic processes, substance abuse, pregnancy, cell line development, epidemiologic studies, etc.
Large marine mammals of the order CETACEA. In the past, they were commercially valued for whale oil, for their flesh as human food and in ANIMAL FEED and FERTILIZERS, and for baleen. Today, there is a moratorium on most commercial whaling, as all species are either listed as endangered or threatened.
Separation technique in which the stationary phase consists of ion exchange resins. The resins contain loosely held small ions that easily exchange places with other small ions of like charge present in solutions washed over the resins.
A subtype of DIABETES MELLITUS that is characterized by INSULIN deficiency. It is manifested by the sudden onset of severe HYPERGLYCEMIA, rapid progression to DIABETIC KETOACIDOSIS, and DEATH unless treated with insulin. The disease may occur at any age, but is most common in childhood or adolescence.
An essential amino acid that is required for the production of HISTAMINE.
A hemoglobin-like oxygen-binding hemeprotein present in the nitrogen-fixing root nodules of leguminous plants. The red pigment has a molecular weight approximately 1/4 that of hemoglobin and has been suggested to act as an oxido-reduction catalyst in symbiotic nitrogen fixation.
An aspect of personal behavior or lifestyle, environmental exposure, or inborn or inherited characteristic, which, on the basis of epidemiologic evidence, is known to be associated with a health-related condition considered important to prevent.
Substances which lower blood glucose levels.
A vertical distance measured from a known level on the surface of a planet or other celestial body.
A myeloproliferative disorder characterized by neoplastic proliferation of erythroblastic and myeloblastic elements with atypical erythroblasts and myeloblasts in the peripheral blood.
An iron-binding beta1-globulin that is synthesized in the LIVER and secreted into the blood. It plays a central role in the transport of IRON throughout the circulation. A variety of transferrin isoforms exist in humans, including some that are considered markers for specific disease states.
Hemolytic anemia due to various intrinsic defects of the erythrocyte.
A major protein in the BLOOD. It is important in maintaining the colloidal osmotic pressure and transporting large organic molecules.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
Studies used to test etiologic hypotheses in which inferences about an exposure to putative causal factors are derived from data relating to characteristics of persons under study or to events or experiences in their past. The essential feature is that some of the persons under study have the disease or outcome of interest and their characteristics are compared with those of unaffected persons.
RED BLOOD CELL sensitivity to change in OSMOTIC PRESSURE. When exposed to a hypotonic concentration of sodium in a solution, red cells take in more water, swell until the capacity of the cell membrane is exceeded, and burst.
The status during which female mammals carry their developing young (EMBRYOS or FETUSES) in utero before birth, beginning from FERTILIZATION to BIRTH.
Puncture of a vein to draw blood for therapeutic purposes. Bloodletting therapy has been used in Talmudic and Indian medicine since the medieval time, and was still practiced widely in the 18th and 19th centuries. Its modern counterpart is PHLEBOTOMY.
The range or frequency distribution of a measurement in a population (of organisms, organs or things) that has not been selected for the presence of disease or abnormality.
Immature, nucleated ERYTHROCYTES occupying the stage of ERYTHROPOIESIS that follows formation of ERYTHROID PRECURSOR CELLS and precedes formation of RETICULOCYTES. The normal series is called normoblasts. Cells called MEGALOBLASTS are a pathologic series of erythroblasts.
State of the body in relation to the consumption and utilization of nutrients.
The cells in the erythroid series derived from MYELOID PROGENITOR CELLS or from the bi-potential MEGAKARYOCYTE-ERYTHROID PROGENITOR CELLS which eventually give rise to mature RED BLOOD CELLS. The erythroid progenitor cells develop in two phases: erythroid burst-forming units (BFU-E) followed by erythroid colony-forming units (CFU-E); BFU-E differentiate into CFU-E on stimulation by ERYTHROPOIETIN, and then further differentiate into ERYTHROBLASTS when stimulated by other factors.
The rate at which oxygen is used by a tissue; microliters of oxygen STPD used per milligram of tissue per hour; the rate at which oxygen enters the blood from alveolar gas, equal in the steady state to the consumption of oxygen by tissue metabolism throughout the body. (Stedman, 25th ed, p346)
Stable chromium atoms that have the same atomic number as the element chromium, but differ in atomic weight. Cr-50, 53, and 54 are stable chromium isotopes.
The presence of methemoglobin in the blood, resulting in cyanosis. A small amount of methemoglobin is present in the blood normally, but injury or toxic agents convert a larger proportion of hemoglobin into methemoglobin, which does not function reversibly as an oxygen carrier. Methemoglobinemia may be due to a defect in the enzyme NADH methemoglobin reductase (an autosomal recessive trait) or to an abnormality in hemoglobin M (an autosomal dominant trait). (Dorland, 27th ed)
Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.
A genus of trematode liver flukes of the family Dicrocoeliidae which includes the species dendriticum and hospes. It occurs in the biliary passages or liver of many vertebrates including man. The intermediate hosts are mainly mollusks but occasionally ants.
Proteins that are present in blood serum, including SERUM ALBUMIN; BLOOD COAGULATION FACTORS; and many other types of proteins.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
Ability of ERYTHROCYTES to change shape as they pass through narrow spaces, such as the microvasculature.

Coupling of the oxygen-linked interaction energy for inositol hexakisphosphate and bezafibrate binding to human HbA0. (1/606)

The energetics of signal propagation between different functional domains (i.e. the binding sites for O2, inositol hexakisphospate (IHP), and bezafibrate (BZF)) of human HbA0 was analyzed at different heme ligation states and through the use of a stable, partially heme ligated intermediate. Present data allow three main conclusions to be drawn, and namely: (i) IHP and BZF enhance each others binding as the oxygenation proceeds, the coupling free energy going from close to zero in the deoxy state to -3.4 kJ/mol in the oxygenated form; (ii) the simultaneous presence of IHP and BZF stabilizes the hemoglobin T quaternary structure at very low O2 pressures, but as oxygenation proceeds it does not impair the transition toward the R structure, which indeed occurs also under these conditions; (iii) under room air pressure (i.e. pO2 = 150 torr), IHP and BZF together induce the formation of an asymmetric dioxygenated hemoglobin tetramer, whose features appear reminiscent of those suggested for transition state species (i.e. T- and R-like tertiary conformation(s) within a quaternary R-like structure).  (+info)

Altered ligand rebinding kinetics due to distal-side effects in hemoglobin chico (Lysbeta66(E10) --> thr). (2/606)

Hb Chico is an unusual human hemoglobin variant that has lowered oxygen affinity, but unaltered cooperativity and anion sensitivity. Previous studies showed these features to be associated with distal-side heme pocket alterations that confer increased structural rigidity on the molecule and that increase water content in the beta-chain heme pocket. We report here that the extent of nanosecond geminate rebinding of oxygen to the variant and its isolated beta-chains is appreciably decreased. Structural alterations in this variant decrease its oxygen recombination rates without significantly altering rates of migration out of the heme pocket. Data analysis indicates that one or more barriers that impede rebinding of oxygen from docking sites in the heme pocket are increased, with less consequence for CO rebinding. Resonance Raman spectra show no significant alterations in spectral regions sensitive to interactions between the heme iron and the proximal histidine residue, confirming that the functional differences in the variant are due to distal-side heme pocket alterations. These effects are discussed in the context of a schematic representation of heme pocket wells and barriers that could aid the design of novel hemoglobins with altered ligand affinity without loss of the normal allosteric responses that facilitate unloading of oxygen to respiring tissues.  (+info)

Sickle hemoglobin polymer melting in high concentration phosphate buffer. (3/606)

Sickle cell hemoglobin (HbS) prepared in argon-saturated 1.8 M phosphate buffer was rapidly mixed with carbon monoxide (CO)-saturated buffer. The binding of CO to the sickle hemoglobin and the simultaneous melting of the hemoglobin polymers were monitored by transmission spectroscopy (optical absorption and turbidity). Changes in the absorption profile were interpreted as resulting from CO binding to deoxy-HbS while reduced scattering (turbidity) was attributed to melting (depolymerization) of the HbS polymer phase. Analysis of the data provides insight into the mechanism and kinetics of sickle hemoglobin polymer melting. Conversion of normal deoxygenated, adult hemoglobin (HbA) in high concentration phosphate buffer to the HbA-CO adduct was characterized by an average rate of 83 s-1. Under the same conditions, conversion of deoxy-HbS in the polymer phase to the HbS-CO adduct in the solution phase is characterized by an average rate of 5.8 s-1 via an intermediate species that grows in with a 36 s-1 rate. Spectral analysis of the intermediate species suggests that a significant amount of CO may bind to the polymer phase before the polymer melts.  (+info)

Physiological effects of modified hemoglobin as an oxygen-carrying macromolecule. (4/606)

A stabilized hemoglobin as oxygen-carrying macromolecules was developed. It had approximately 90,000 dalton molecular weights and its intravascular half life was 36 hours. Its molecular size was less than 0.1 micron. Its hemoglobin concentration was 6% and P50 value was 24 mmHg. The oxygen carried inside the plasma performs differently than the oxygen carried inside the red cells. Only less than 0.3 ml of oxygen in 100 ml of blood is available inside the plasma while 14-19 ml of oxygen is carried inside the red cells. Thus, less than 5 ml of oxygen is available inside the plasma of the entire body. When a patient develops hypovolemic shock, the red cells are bypassed and are not perfused directly inside the tissues. However, the plasma should reach such hypoxic tissues. Thus, infusion of oxygen-carrying macromolecules in the plasma should be therapeutically effective even if less than 100 ml of stabilized hemoglobin solution were infused under shock conditions. The basic physiology of oxygen-carrying macromolecules is described in detail, which is different from the oxygen carried inside the red cells.  (+info)

Metal complexes as allosteric effectors of human hemoglobin: an NMR study of the interaction of the gadolinium(III) bis(m-boroxyphenylamide)diethylenetriaminepentaacetic acid complex with human oxygenated and deoxygenated hemoglobin. (5/606)

The boronic functionalities on the outer surface of the Gd(III) bis(m-boroxyphenylamide)DTPA complex (Gd(III)L) enable it to bind to fructosamine residues of oxygenated glycated human adult hemoglobin. The formation of the macromolecular adduct can be assessed by NMR spectroscopy via observation of the enhancement of the solvent water proton relaxation rate. Unexpectedly, a strong binding interaction was also observed for the oxygenated unglycated human adult hemoglobin, eventually displaying a much higher relaxation enhancement. From relaxation rate measurements it was found that two Gd(III)L complexes interact with one hemoglobin tetramer (KD = 1.0 x 10(-5) M and 4.6 x 10(-4) M, respectively), whereas no interaction has been observed with monomeric hemoproteins. A markedly higher affinity of the Gd(III)L complex has been observed for oxygenated and aquo-met human adult hemoglobin derivatives with respect to the corresponding deoxy derivative. Upon binding, a net change in the quaternary structure of hemoglobin has been assessed by monitoring the changes in the high-resolution 1H-NMR spectrum of the protein as well as in the Soret absorption band. On the basis of these observations and the 11B NMR results obtained with the diamagnetic La(III)L complex, we suggest that the interaction between the lanthanide complex and deoxygenated, oxygenated, and aquo-met derivatives of human adult hemoglobin takes place at the 2, 3-diphosphoglycerate (DPG) binding site, through the formation of N-->B coordinative bonds at His143beta and His2beta residues of different beta-chains. The stronger binding to the oxygenated form is then responsible for a shift of the allosteric equilibrium toward the high-affinity R-state. Accordingly, Gd(III)L affinity for oxygenated human fetal hemoglobin (lacking His143beta) is significantly lower than that observed for the unglycated human adult tetramer.  (+info)

Fetal hemoglobin (HbF) synthesis in baboons, Papio cynocephalus. Analysis of fetal and adult hemoglobin synthesis during fetal development. (6/606)

Fetal hemoglobin (HbF) and adult hemoglobin (HbA) synthesis was studied in fetal baboons, Papio cynocephalus, to determine the normal pattern of hemoglobin production during fetal development. Fetuses ranging from 53 to 180 days gestation (term gestation 184 days) were used. Erythroid cells were incubated with 3H-L-leucine, and the rates of globin chain synthesis and the distribution of radioactivity into hemoglobin intermediates and completed hemoglobin molecules were determined. Gamma chain synthesis accounted for approximately 97% of the total nonalpha chain synthesis up to 140 days gestation; beta chain synthesis accounted for the remainder. After 140 days gestation, approximately equal quantities of gamma and beta chain were synthesized in the bone marrow. Prior to 140 days gestation, total alpha chain synthesis was 30% greater than total non-alpha chain synthesis, while there was balanced chain synthesis after 140 days gestation. During the period of excess alpha chain synthesis, fetal erythrocytes contained a large pool of alpha-hemoglobin (alpha chain with heme attached) molecules uncombined with beta or gamma chains. In view of the possibility that alpha chains may have a lower affinity for gamma chains than beta chains, excess alpha chain synthesis may be required to maintain low levels of free gamma chains.  (+info)

Kinetic studies on the binding affinity of human hemoglobin for the 4th carbon monoxide molecule, L4. (7/606)

L4, the affinity of hemoglobin for the 4th CO molecule, has been determined for human adult hemoglobin (HbA) as a function of pH and the presence of organic phosphates by measuring the kinetic parameters for the reaction. l'4, the rate of combination of CO with the triliganded molecule, was measured by flash photolysis while l4, the rate of CO dissociation for the ligand-saturated molecule, was measured by ligand replacement. L4 is pH-dependent and affected by 2,3-diphosphoglycerate. Additionally, this pH dependence of the high affinity state is largely eliminated by carboxypeptidase A digestion. L4 for human fetal hemoglobin (HbF) in phosphate buffers was also determined and found to be pH-dependent. These results cannot be reconciled within the framework of the two-state allosteric model. Additional structures in the conformational equilibrium due to either intermediates in the T to R transition or two or more R states must exist.  (+info)

Iron nutritional status in preterm infants fed formulas fortified with iron. (8/606)

AIMS: To prospectively evaluate the iron nutritional status of preterm infants fed either a term (0.5 mg/dl iron) or preterm (0.9 mg/dl) formulas fortified with iron after hospital discharge. METHODS: Healthy low birthweight preterm infants were randomly assigned into three groups at the time of hospital discharge. Group A were fed an iron fortified preterm formula (0.9 mg/dl iron) until 6 months corrected age; group B, a fortified term formula (0.5 mg/l iron) until 6 months corrected age group C, the preterm formula between hospital discharge and term, then the term formula until 6 months corrected age. RESULTS: Seventy eight infants were followed up to 6 months corrected age. Iron intake from formula differed significantly between the groups (A, 1.17 mg/kg/day (SD 0.32) > C, 0. 86 mg/kg/day (SD 0.40) = B, 0.81 mg/kg/day (SD 0.23); p < 0.0001). Haemoglobin concentrations were similar to those of iron sufficient preterm infants of the same postnatal age, and term infants of the same postmenstrual age (after 3 months of age). There were no significant differences in haemoglobin concentration (p = 0.391), plasma ferritin (A vs B, p = 0.322), or in the incidence of iron deficiency (A vs B, p = 0.534). CONCLUSIONS: Iron fortified formulas containing between 0.5 and 0.9 mg/dl iron seem to meet the iron nutritional needs of preterm infants after hospital discharge.  (+info)

Hemoglobin (Hb or Hgb) is the main oxygen-carrying protein in the red blood cells, which are responsible for delivering oxygen throughout the body. It is a complex molecule made up of four globin proteins and four heme groups. Each heme group contains an iron atom that binds to one molecule of oxygen. Hemoglobin plays a crucial role in the transport of oxygen from the lungs to the body's tissues, and also helps to carry carbon dioxide back to the lungs for exhalation.

There are several types of hemoglobin present in the human body, including:

* Hemoglobin A (HbA): This is the most common type of hemoglobin, making up about 95-98% of total hemoglobin in adults. It consists of two alpha and two beta globin chains.
* Hemoglobin A2 (HbA2): This makes up about 1.5-3.5% of total hemoglobin in adults. It consists of two alpha and two delta globin chains.
* Hemoglobin F (HbF): This is the main type of hemoglobin present in fetal life, but it persists at low levels in adults. It consists of two alpha and two gamma globin chains.
* Hemoglobin S (HbS): This is an abnormal form of hemoglobin that can cause sickle cell disease when it occurs in the homozygous state (i.e., both copies of the gene are affected). It results from a single amino acid substitution in the beta globin chain.
* Hemoglobin C (HbC): This is another abnormal form of hemoglobin that can cause mild to moderate hemolytic anemia when it occurs in the homozygous state. It results from a different single amino acid substitution in the beta globin chain than HbS.

Abnormal forms of hemoglobin, such as HbS and HbC, can lead to various clinical disorders, including sickle cell disease, thalassemia, and other hemoglobinopathies.

Hemoglobin A is the most common form of hemoglobin, which is the oxygen-carrying protein in red blood cells. Hemoglobin A is a tetramer composed of two alpha and two beta globin chains, each containing a heme group that binds to oxygen. It is typically measured in laboratory tests to assess for various medical conditions such as anemia or diabetes. In the context of diabetes, the measurement of hemoglobin A1c (a form of hemoglobin A that is glycated or bound to glucose) is used to monitor long-term blood sugar control.

Abnormal hemoglobins refer to variants of the oxygen-carrying protein found in red blood cells, which differ from the normal adult hemoglobin (HbA) in terms of their structure and function. These variations can result from genetic mutations that affect the composition of the globin chains in the hemoglobin molecule. Some abnormal hemoglobins are clinically insignificant, while others can lead to various medical conditions such as hemolytic anemia, thalassemia, or sickle cell disease. Examples of abnormal hemoglobins include HbS (associated with sickle cell anemia), HbC, HbE, and HbF (fetal hemoglobin). These variants can be detected through specialized laboratory tests, such as hemoglobin electrophoresis or high-performance liquid chromatography (HPLC).

Fetal hemoglobin (HbF) is a type of hemoglobin that is produced in the fetus and newborn babies. It is composed of two alpha-like globin chains and two gamma-globin chains, designated as α2γ2. HbF is the primary form of hemoglobin during fetal development, replacing the embryonic hemoglobin (HbG) around the eighth week of gestation.

The unique property of HbF is its higher affinity for oxygen compared to adult hemoglobin (HbA), which helps ensure adequate oxygen supply from the mother to the developing fetus. After birth, as the newborn starts breathing on its own and begins to receive oxygen directly, the production of HbF gradually decreases and is usually replaced by HbA within the first year of life.

In some genetic disorders like sickle cell disease and beta-thalassemia, persistence of HbF into adulthood can be beneficial as it reduces the severity of symptoms due to its higher oxygen-carrying capacity and less polymerization tendency compared to HbS (in sickle cell disease) or unpaired alpha chains (in beta-thalassemia). Treatments like hydroxyurea are used to induce HbF production in these patients as a therapeutic approach.

Hemoglobin S (HbS) is a genetic variant of hemoglobin, which is the oxygen-carrying protein in red blood cells. This abnormal form of hemogllobin results from a mutation in the beta-globin gene, leading to the substitution of valine for glutamic acid at position six of the beta-globin chain.

In individuals with sickle cell disease (a group of inherited red blood cell disorders), both copies of their beta-globin genes carry this mutation, causing the majority of their hemoglobin to be HbS. When deoxygenated, HbS molecules have a tendency to polymerize and form long, rigid rods within the red blood cells, distorting their shape into a characteristic sickle or crescent form.

These sickled red blood cells are less flexible and more prone to rupture (hemolysis), leading to chronic anemia, vaso-occlusive crises, and other disease complications. Sickle cell disease primarily affects people of African, Mediterranean, Middle Eastern, and Indian ancestry, but it can also be found in other populations worldwide.

Hemoglobin C is a type of hemoglobin variant, which is the oxygen-carrying protein in red blood cells. Hemoglobin C is caused by a specific genetic mutation that results in the substitution of lysine for glutamic acid at position 6 on the beta globin chain of the hemoglobin molecule.

This variant is often associated with a benign condition known as hemoglobin C trait, where an individual inherits one copy of the mutated gene from one parent and one normal gene from the other parent. People with this trait usually have no symptoms or only mild anemia, if any. However, if an individual inherits two copies of the Hemoglobin C gene (one from each parent), they will have a more severe form of hemoglobin disorder called Hemoglobin CC disease, which can cause mild to moderate hemolytic anemia and other complications.

It's important to note that Hemoglobin C is most commonly found in people of West African descent, but it can also occur in other populations with African ancestry.

Oxyhemoglobin is the form of hemoglobin that is combined with oxygen in red blood cells. It's created when oxygen molecules bind to the iron-containing heme groups of the hemoglobin protein inside the lungs, allowing for the transportation of oxygen from the lungs to body tissues. The affinity of hemoglobin for oxygen is influenced by factors such as pH, carbon dioxide concentration, and temperature, which can affect the release of oxygen from oxyhemoglobin in different parts of the body based on their specific needs.

Glycosylated Hemoglobin A, also known as Hemoglobin A1c or HbA1c, is a form of hemoglobin that is bound to glucose. It is formed in a non-enzymatic glycation reaction with glucose in the blood. The amount of this hemoglobin present in the blood is proportional to the average plasma glucose concentration over the previous 8-12 weeks, making it a useful indicator for monitoring long-term blood glucose control in people with diabetes mellitus.

In other words, HbA1c reflects the integrated effects of glucose regulation over time and is an important clinical marker for assessing glycemic control and risk of diabetic complications. The normal range for HbA1c in individuals without diabetes is typically less than 5.7%, while a value greater than 6.5% is indicative of diabetes.

Hemoglobin E (HbE) is a structural variant of hemoglobin, which is the oxygen-carrying protein in red blood cells. This variant results from a specific mutation in the beta-globin gene, leading to the substitution of glutamic acid with lysine at position 26 of the beta-globin chain.

HbE is most commonly found in people from Southeast Asia, particularly in populations from Thailand, Cambodia, and Laos. It can also be found in other parts of the world, such as India, Bangladesh, and Pakistan. HbE is usually asymptomatic when it occurs in its heterozygous form (one normal beta-globin gene and one HbE gene). However, when it occurs in the homozygous form (two HbE genes), or in combination with other hemoglobinopathies like thalassemia, it can lead to a range of clinical manifestations, including mild to severe microcytic anemia, splenomegaly, and jaundice.

Individuals with HbE may have increased susceptibility to certain infections and may experience complications during pregnancy or surgery due to impaired oxygen-carrying capacity. Regular monitoring of hemoglobin levels, iron status, and potential complications is essential for managing individuals with Hemoglobin E effectively.

Hemoglobin A2 is a type of hemoglobin that is found in human red blood cells. Hemoglobin is the protein in red blood cells that carries oxygen throughout the body. Hemoglobin A2 is made up of two alpha-like globin chains and two delta-globin chains, and it accounts for approximately 1.5 to 3.5% of the total hemoglobin in adult humans.

Hemoglobin A2 is not normally present in significant amounts until after a child has passed through their first year of life. Its level remains relatively constant throughout adulthood, and it is often used as a diagnostic marker for certain types of anemia, such as beta-thalassemia. In people with beta-thalassemia, the production of beta-globin chains is reduced or absent, leading to an increase in the relative proportion of Hemoglobin A2 and Hemoglobin F (fetal hemoglobin) in the red blood cells.

It's important to note that Hemoglobin A2 measurement alone is not enough for a definitive diagnosis of beta-thalassemia, but it can be used as a supportive test along with other investigations such as complete blood count (CBC), hemoglobin electrophoresis and molecular genetic testing.

Methemoglobin is a form of hemoglobin in which the iron within the heme group is in the ferric (Fe3+) state instead of the ferrous (Fe2+) state. This oxidation reduces its ability to bind and transport oxygen effectively, leading to methemoglobinemia when methemoglobin levels become too high. Methemoglobin has a limited capacity to release oxygen to tissues, which can result in hypoxia (reduced oxygen supply) and cyanosis (bluish discoloration of the skin and mucous membranes).

Methemoglobin is normally present in small amounts in the blood, but certain factors such as exposure to oxidizing agents, genetic predisposition, or certain medications can increase its levels. Elevated methemoglobin levels can be treated with methylene blue, which helps restore the iron within hemoglobin back to its ferrous state and improves oxygen transport capacity.

Truncated hemoglobins are a group of hemoglobin variants that lack the normal C-terminal extension of the beta-globin chain. They were first identified in organisms living in extreme environments, such as bacteria found in deep-sea hydrothermal vents and in animals adapted to high-altitude hypoxia. These hemoglobins have unique structural and functional properties that allow them to function efficiently under low oxygen concentrations.

Truncated hemoglobins are characterized by the absence of the last 1-3 amino acids at the C-terminus of the beta-globin chain, which results in a more compact structure compared to normal hemoglobin. This structural difference leads to altered oxygen binding properties and increased stability under extreme conditions.

Truncated hemoglobins have been studied for their potential applications in biotechnology and medicine, particularly in the development of new strategies for the treatment of hypoxia-related disorders such as ischemia, stroke, and cancer. However, further research is needed to fully understand their mechanisms of action and therapeutic potential.

Anemia is a medical condition characterized by a lower than normal number of red blood cells or lower than normal levels of hemoglobin in the blood. Hemoglobin is an important protein in red blood cells that carries oxygen from the lungs to the rest of the body. Anemia can cause fatigue, weakness, shortness of breath, and a pale complexion because the body's tissues are not getting enough oxygen.

Anemia can be caused by various factors, including nutritional deficiencies (such as iron, vitamin B12, or folate deficiency), blood loss, chronic diseases (such as kidney disease or rheumatoid arthritis), inherited genetic disorders (such as sickle cell anemia or thalassemia), and certain medications.

There are different types of anemia, classified based on the underlying cause, size and shape of red blood cells, and the level of hemoglobin in the blood. Treatment for anemia depends on the underlying cause and may include dietary changes, supplements, medication, or blood transfusions.

Hemoglobinopathies are a group of genetic disorders characterized by structural or functional abnormalities of the hemoglobin molecule in red blood cells. Hemoglobin is a complex protein that plays a crucial role in carrying oxygen throughout the body. The two most common types of hemoglobinopathies are sickle cell disease and thalassemia.

In sickle cell disease, a single mutation in the beta-globin gene results in the production of an abnormal form of hemoglobin called hemoglobin S (HbS). When deoxygenated, HbS molecules tend to aggregate and form long polymers, causing the red blood cells to become sickle-shaped, rigid, and fragile. These abnormally shaped cells can block small blood vessels, leading to tissue damage, chronic pain, organ dysfunction, and other serious complications.

Thalassemias are a heterogeneous group of disorders caused by mutations in the genes that regulate the production of alpha- or beta-globin chains. These mutations result in reduced or absent synthesis of one or more globin chains, leading to an imbalance in hemoglobin composition and structure. This imbalance can cause premature destruction of red blood cells (hemolysis), resulting in anemia, jaundice, splenomegaly, and other symptoms.

Hemoglobinopathies are typically inherited in an autosomal recessive manner, meaning that affected individuals have two copies of the abnormal gene – one from each parent. Carriers of a single abnormal gene usually do not show any signs or symptoms of the disorder but can pass the abnormal gene on to their offspring.

Early diagnosis and appropriate management of hemoglobinopathies are essential for improving quality of life, reducing complications, and increasing survival rates. Treatment options may include blood transfusions, iron chelation therapy, antibiotics, pain management, and, in some cases, bone marrow transplantation or gene therapy.

Carboxyhemoglobin (COHb) is a form of hemoglobin that has bonded with carbon monoxide (CO), a colorless, odorless gas. Normally, hemoglobin in red blood cells binds with oxygen (O2) to carry it throughout the body. However, when exposed to CO, hemoglobin preferentially binds with it, forming carboxyhemoglobin, which reduces the amount of oxygen that can be carried by the blood. This can lead to hypoxia (lack of oxygen in tissues) and potentially serious medical consequences, including death. Carbon monoxide exposure can occur from sources such as smoke inhalation, vehicle exhaust, or faulty heating systems.

Hemoglobinometry is a method used to measure the amount or concentration of hemoglobin (Hb) in blood. Hemoglobin is a protein in red blood cells that carries oxygen throughout the body. Hemoglobinometry is typically performed on a sample of whole blood and can be done using various methods, including spectrophotometry, colorimetry, or automated analyzers.

The results of hemoglobinometry are reported in units of grams per deciliter (g/dL) or grams per liter (g/L). Normal values for hemoglobin concentration vary depending on factors such as age, sex, and altitude, but in general, a healthy adult male should have a hemoglobin level between 13.5 and 17.5 g/dL, while a healthy adult female should have a level between 12.0 and 15.5 g/dL.

Hemoglobinometry is an important diagnostic tool in the evaluation of various medical conditions, including anemia, polycythemia, and respiratory disorders. It can help identify the cause of symptoms such as fatigue, shortness of breath, or dizziness and guide treatment decisions.

Oxygen is a colorless, odorless, tasteless gas that constitutes about 21% of the earth's atmosphere. It is a crucial element for human and most living organisms as it is vital for respiration. Inhaled oxygen enters the lungs and binds to hemoglobin in red blood cells, which carries it to tissues throughout the body where it is used to convert nutrients into energy and carbon dioxide, a waste product that is exhaled.

Medically, supplemental oxygen therapy may be provided to patients with conditions such as chronic obstructive pulmonary disease (COPD), pneumonia, heart failure, or other medical conditions that impair the body's ability to extract sufficient oxygen from the air. Oxygen can be administered through various devices, including nasal cannulas, face masks, and ventilators.

Hemoglobin C disease is a genetic disorder that affects the structure and function of hemoglobin, a protein in red blood cells responsible for carrying oxygen throughout the body. The disease is caused by a mutation in the gene that produces the beta-globin chain of hemoglobin, resulting in the production of an abnormal form of hemoglobin called Hemoglobin C (HbC).

People with Hemoglobin C disease inherit one copy of the HbC gene from each parent. This means they have two copies of the mutated gene and produce mostly Hemoglobin C, instead of the normal Hemoglobin A. The presence of Hemoglobin C can cause the red blood cells to become rigid and fragile, leading to a condition called hemolytic anemia.

Symptoms of Hemoglobin C disease may include fatigue, weakness, shortness of breath, pale skin, jaundice, and dark urine. The severity of the symptoms can vary widely from person to person, with some individuals experiencing mild symptoms and others having more severe complications.

Hemoglobin C disease is a chronic condition that requires ongoing medical management, including regular monitoring of hemoglobin levels, iron status, and other blood parameters. Treatment may include blood transfusions, folic acid supplementation, and medications to manage symptoms such as anemia and pain.

It's important to note that Hemoglobin C disease is not the same as sickle cell disease, which is another genetic disorder that affects hemoglobin structure and function. While both conditions can cause hemolytic anemia, they are caused by different mutations in the beta-globin gene and have distinct clinical features and management approaches.

Blood substitutes, also known as artificial blood or blood surrogates, are fluids that are designed to mimic some of the properties and functions of human blood. They are used as a replacement for blood transfusions in situations where blood is not available or when it is not safe to use. Blood substitutes can be divided into two main categories: oxygen-carrying and non-oxygen-carrying.

Oxygen-carrying blood substitutes contain artificial molecules called hemoglobin-based oxygen carriers (HBOCs) that are designed to carry oxygen from the lungs to the body's tissues. These HBOCs can be derived from human or animal hemoglobin, or they can be synthetically produced.

Non-oxygen-carrying blood substitutes, on the other hand, do not contain hemoglobin and are used primarily to restore intravascular volume and maintain blood pressure in cases of hypovolemia (low blood volume) caused by bleeding or dehydration. These products include crystalloids, such as saline solution and lactated Ringer's solution, and colloids, such as albumin and hydroxyethyl starch solutions.

It is important to note that while blood substitutes can be useful in certain situations, they are not a perfect substitute for human blood. They do not provide all of the functions of blood, such as immune defense and clotting, and their use is associated with some risks, including allergic reactions, kidney damage, and increased oxygen free radical production. Therefore, they should only be used when there is no suitable alternative available.

Hemoglobin J is a variant form of hemoglobin, which is the oxygen-carrying protein in red blood cells. This variant is caused by a specific mutation in the gene for the beta-globin chain, one of the two types of chains that make up hemoglobin.

The mutation responsible for Hemoglobin J results in the substitution of a glutamic acid residue with a valine residue at position 6 of the beta-globin chain. This change can lead to the formation of abnormal hemoglobin molecules that can cause red blood cells to become fragile and susceptible to rupture, a condition known as hemolysis.

Hemoglobin J is typically detected during routine newborn screening or through diagnostic testing for hemoglobin disorders. While Hemoglobin J itself is not considered a disease-causing variant, individuals who inherit it in combination with other abnormal hemoglobin genes may be at risk for developing hemolytic anemia or other related conditions.

Hemoglobin H (Hb H) is a type of abnormal hemoglobin that can occur in individuals with certain genetic disorders, such as hemoglobinopathies. It is formed when four beta-globin chains come together, instead of the usual two alpha and two beta chains found in normal adult hemoglobin (Hb A).

This abnormal structure can result from a mutation that causes the absence or deficiency of alpha-globin chains, leading to an excess of beta-globin chains. Hemoglobin H is often associated with conditions such as thalassemia, particularly when there is a severe deficiency of alpha-globin chain production (alpha-thalassemia).

Hemoglobin H can cause hemolytic anemia, which means that the red blood cells are destroyed prematurely. The severity of the condition depends on the degree of imbalance between alpha and beta chains and other genetic factors. Symptoms may include fatigue, jaundice, and splenomegaly (enlarged spleen).

Diphosphoglycerates (also known as 2,3-diphosphoglycerates or 2,3-DPG) are organic molecules found in red blood cells. They play a crucial role in regulating the affinity of hemoglobin for oxygen. Hemoglobin is the protein in red blood cells that carries oxygen from the lungs to the body's tissues.

When the concentration of diphosphoglycerates in red blood cells increases, it reduces the ability of hemoglobin to bind with oxygen, which allows more oxygen to be released into the tissues. This is particularly important in conditions where there is low oxygen availability, such as at high altitudes or in diseases that cause poor oxygen delivery to the tissues, like heart failure and chronic obstructive pulmonary disease (COPD).

In summary, diphosphoglycerates are essential molecules that help regulate hemoglobin's affinity for oxygen, ensuring optimal oxygen delivery to the body's tissues.

Sickle cell anemia is a genetic disorder that affects the hemoglobin in red blood cells. Hemoglobin is responsible for carrying oxygen throughout the body. In sickle cell anemia, the hemoglobin is abnormal and causes the red blood cells to take on a sickle shape, rather than the normal disc shape. These sickled cells are stiff and sticky, and they can block blood vessels, causing tissue damage and pain. They also die more quickly than normal red blood cells, leading to anemia.

People with sickle cell anemia often experience fatigue, chronic pain, and jaundice. They may also have a higher risk of infections and complications such as stroke, acute chest syndrome, and priapism. The disease is inherited from both parents, who must both be carriers of the sickle cell gene. It primarily affects people of African descent, but it can also affect people from other ethnic backgrounds.

There is no cure for sickle cell anemia, but treatments such as blood transfusions, medications to manage pain and prevent complications, and bone marrow transplantation can help improve quality of life for affected individuals. Regular medical care and monitoring are essential for managing the disease effectively.

Erythrocytes, also known as red blood cells (RBCs), are the most common type of blood cell in circulating blood in mammals. They are responsible for transporting oxygen from the lungs to the body's tissues and carbon dioxide from the tissues to the lungs.

Erythrocytes are formed in the bone marrow and have a biconcave shape, which allows them to fold and bend easily as they pass through narrow blood vessels. They do not have a nucleus or mitochondria, which makes them more flexible but also limits their ability to reproduce or repair themselves.

In humans, erythrocytes are typically disc-shaped and measure about 7 micrometers in diameter. They contain the protein hemoglobin, which binds to oxygen and gives blood its red color. The lifespan of an erythrocyte is approximately 120 days, after which it is broken down in the liver and spleen.

Abnormalities in erythrocyte count or function can lead to various medical conditions, such as anemia, polycythemia, and sickle cell disease.

2,3-Diphosphoglycerate (2,3-DPG) is a molecule found in red blood cells that plays a crucial role in regulating the affinity of hemoglobin for oxygen. It is a byproduct of the glycolytic pathway, which is a series of biochemical reactions that convert glucose into energy.

In the tissues where oxygen demand is high, such as muscles and organs, 2,3-DPG concentrations are typically elevated. This molecule binds to deoxygenated hemoglobin at specific sites on the beta chains, reducing its affinity for oxygen and promoting the release of oxygen to the tissues.

Conversely, in the lungs where oxygen is abundant, 2,3-DPG concentrations are lower, allowing hemoglobin to bind more readily to oxygen and load up with oxygen for delivery to the tissues. Therefore, 2,3-DPG helps optimize the matching of oxygen supply and demand in the body.

Globins are a group of proteins that contain a heme prosthetic group, which binds and transports oxygen in the blood. The most well-known globin is hemoglobin, which is found in red blood cells and is responsible for carrying oxygen from the lungs to the body's tissues. Other members of the globin family include myoglobin, which is found in muscle tissue and stores oxygen, and neuroglobin and cytoglobin, which are found in the brain and other organs and may have roles in protecting against oxidative stress and hypoxia (low oxygen levels). Globins share a similar structure, with a folded protein surrounding a central heme group. Mutations in globin genes can lead to various diseases, such as sickle cell anemia and thalassemia.

Heme is not a medical term per se, but it is a term used in the field of medicine and biology. Heme is a prosthetic group found in hemoproteins, which are proteins that contain a heme iron complex. This complex plays a crucial role in various biological processes, including oxygen transport (in hemoglobin), electron transfer (in cytochromes), and chemical catalysis (in peroxidases and catalases).

The heme group consists of an organic component called a porphyrin ring, which binds to a central iron atom. The iron atom can bind or release electrons, making it essential for redox reactions in the body. Heme is also vital for the formation of hemoglobin and myoglobin, proteins responsible for oxygen transport and storage in the blood and muscles, respectively.

In summary, heme is a complex organic-inorganic structure that plays a critical role in several biological processes, particularly in electron transfer and oxygen transport.

Thalassemia is a group of inherited genetic disorders that affect the production of hemoglobin, a protein in red blood cells responsible for carrying oxygen throughout the body. The disorder results in less efficient or abnormal hemoglobin, which can lead to anemia, an insufficient supply of oxygen-rich red blood cells.

There are two main types of Thalassemia: alpha and beta. Alpha thalassemia occurs when there is a problem with the alpha globin chain production, while beta thalassemia results from issues in beta globin chain synthesis. These disorders can range from mild to severe, depending on the number of genes affected and their specific mutations.

Severe forms of Thalassemia may require regular blood transfusions, iron chelation therapy, or even a bone marrow transplant to manage symptoms and prevent complications.

In the context of medicine, iron is an essential micromineral and key component of various proteins and enzymes. It plays a crucial role in oxygen transport, DNA synthesis, and energy production within the body. Iron exists in two main forms: heme and non-heme. Heme iron is derived from hemoglobin and myoglobin in animal products, while non-heme iron comes from plant sources and supplements.

The recommended daily allowance (RDA) for iron varies depending on age, sex, and life stage:

* For men aged 19-50 years, the RDA is 8 mg/day
* For women aged 19-50 years, the RDA is 18 mg/day
* During pregnancy, the RDA increases to 27 mg/day
* During lactation, the RDA for breastfeeding mothers is 9 mg/day

Iron deficiency can lead to anemia, characterized by fatigue, weakness, and shortness of breath. Excessive iron intake may result in iron overload, causing damage to organs such as the liver and heart. Balanced iron levels are essential for maintaining optimal health.

Hematocrit is a medical term that refers to the percentage of total blood volume that is made up of red blood cells. It is typically measured as part of a complete blood count (CBC) test. A high hematocrit may indicate conditions such as dehydration, polycythemia, or living at high altitudes, while a low hematocrit may be a sign of anemia, bleeding, or overhydration. It is important to note that hematocrit values can vary depending on factors such as age, gender, and pregnancy status.

Erythropoietin (EPO) is a hormone that is primarily produced by the kidneys and plays a crucial role in the production of red blood cells in the body. It works by stimulating the bone marrow to produce more red blood cells, which are essential for carrying oxygen to various tissues and organs.

EPO is a glycoprotein that is released into the bloodstream in response to low oxygen levels in the body. When the kidneys detect low oxygen levels, they release EPO, which then travels to the bone marrow and binds to specific receptors on immature red blood cells called erythroblasts. This binding triggers a series of events that promote the maturation and proliferation of erythroblasts, leading to an increase in the production of red blood cells.

In addition to its role in regulating red blood cell production, EPO has also been shown to have neuroprotective effects and may play a role in modulating the immune system. Abnormal levels of EPO have been associated with various medical conditions, including anemia, kidney disease, and certain types of cancer.

EPO is also used as a therapeutic agent for the treatment of anemia caused by chronic kidney disease, chemotherapy, or other conditions that affect red blood cell production. Recombinant human EPO (rhEPO) is a synthetic form of the hormone that is produced using genetic engineering techniques and is commonly used in clinical practice to treat anemia. However, misuse of rhEPO for performance enhancement in sports has been a subject of concern due to its potential to enhance oxygen-carrying capacity and improve endurance.

Hemoglobin SC disease, also known as sickle cell-C disease or SC disorder, is a genetic blood disorder that is a variant of sickle cell anemia. It is caused by the presence of both hemoglobin S (HbS) and hemoglobin C (HbC) in the red blood cells.

Hemoglobin is the protein in red blood cells that carries oxygen throughout the body. In Hemoglobin SC disease, the abnormal HbS and HbC proteins can cause the red blood cells to become rigid, sticky, and C-shaped (sickled), which can lead to blockages in small blood vessels.

Symptoms of Hemoglibin SC disease may include anemia, fatigue, jaundice, episodes of pain (known as sickle cell crises), and an increased risk of infection. The severity of the symptoms can vary widely from person to person. Treatment typically focuses on managing symptoms and preventing complications, and may include medications, blood transfusions, and sometimes a bone marrow transplant.

Carbon monoxide (CO) is a colorless, odorless, and tasteless gas that is slightly less dense than air. It is toxic to hemoglobic animals when encountered in concentrations above about 35 ppm. This compound is a product of incomplete combustion of organic matter, and is a major component of automobile exhaust.

Carbon monoxide is poisonous because it binds to hemoglobin in red blood cells much more strongly than oxygen does, forming carboxyhemoglobin. This prevents the transport of oxygen throughout the body, which can lead to suffocation and death. Symptoms of carbon monoxide poisoning include headache, dizziness, weakness, nausea, vomiting, confusion, and disorientation. Prolonged exposure can lead to unconsciousness and death.

Carbon monoxide detectors are commonly used in homes and other buildings to alert occupants to the presence of this dangerous gas. It is important to ensure that these devices are functioning properly and that they are placed in appropriate locations throughout the building. Additionally, it is essential to maintain appliances and heating systems to prevent the release of carbon monoxide into living spaces.

Hematinics are a class of medications and dietary supplements that are used to enhance the production of red blood cells or hemoglobin in the body. They typically contain iron, vitamin B12, folic acid, or other nutrients that are essential for the synthesis of hemoglobin and the formation of red blood cells.

Iron is a critical component of hematinics because it plays a central role in the production of hemoglobin, which is the protein in red blood cells that carries oxygen throughout the body. Vitamin B12 and folic acid are also important nutrients for red blood cell production, as they help to regulate the growth and division of red blood cells in the bone marrow.

Hematinics are often prescribed to treat anemia, which is a condition characterized by a low red blood cell count or abnormally low levels of hemoglobin in the blood. Anemia can be caused by a variety of factors, including nutritional deficiencies, chronic diseases, and inherited genetic disorders.

Examples of hematinics include ferrous sulfate (an iron supplement), cyanocobalamin (vitamin B12), and folic acid. These medications are available in various forms, such as tablets, capsules, and liquids, and can be taken orally or by injection. It is important to follow the dosage instructions carefully and to inform your healthcare provider of any other medications you are taking, as hematinics can interact with certain drugs and may cause side effects.

Erythrocyte count, also known as red blood cell (RBC) count, is a laboratory test that measures the number of red blood cells in a sample of blood. Red blood cells are important because they carry oxygen from the lungs to the rest of the body. A low erythrocyte count may indicate anemia, while a high count may be a sign of certain medical conditions such as polycythemia. The normal range for erythrocyte count varies depending on a person's age, sex, and other factors.

Erythrocyte indices are a set of calculated values that provide information about the size and hemoglobin content of red blood cells (erythrocytes). These indices are commonly used in the complete blood count (CBC) test to help diagnose various types of anemia and other conditions affecting the red blood cells.

The three main erythrocyte indices are:

1. Mean Corpuscular Volume (MCV): This is the average volume of a single red blood cell, measured in femtoliters (fL). MCV helps to differentiate between microcytic, normocytic, and macrocytic anemia. Microcytic anemia is characterized by low MCV values (100 fL).
2. Mean Corpuscular Hemoglobin (MCH): This is the average amount of hemoglobin present in a single red blood cell, measured in picograms (pg). MCH helps to assess the oxygen-carrying capacity of red blood cells. Low MCH values may indicate hypochromic anemia, where the red blood cells have reduced hemoglobin content.
3. Mean Corpuscular Hemoglobin Concentration (MCHC): This is the average concentration of hemoglobin in a single red blood cell, measured as a percentage. MCHC reflects the hemoglobin concentration relative to the size of the red blood cells. Low MCHC values may indicate hypochromic anemia, while high MCHC values could suggest spherocytosis or other conditions affecting red blood cell shape and integrity.

These erythrocyte indices are calculated based on the red blood cell count, hemoglobin concentration, and hematocrit results obtained from a CBC test. They provide valuable information for healthcare professionals to diagnose and manage various hematological conditions.

Iron-deficiency anemia is a condition characterized by a decrease in the total amount of hemoglobin or red blood cells in the blood, caused by insufficient iron levels in the body. Hemoglobin is a protein in red blood cells that carries oxygen from the lungs to the rest of the body. When iron levels are low, the body cannot produce enough hemoglobin, leading to the production of smaller and fewer red blood cells, known as microcytic hypochromic anemia.

Iron is essential for the production of hemoglobin, and a deficiency in iron can result from inadequate dietary intake, chronic blood loss, or impaired absorption. In addition to fatigue and weakness, symptoms of iron-deficiency anemia may include shortness of breath, headaches, dizziness, pale skin, and brittle nails. Treatment typically involves iron supplementation and addressing the underlying cause of the iron deficiency.

Phytic acid, also known as phytate in its salt form, is a natural substance found in plant-based foods such as grains, legumes, nuts, and seeds. It's a storage form of phosphorus for the plant and is often referred to as an "anti-nutrient" because it can bind to certain minerals like calcium, iron, magnesium, and zinc in the gastrointestinal tract and prevent their absorption. This can potentially lead to mineral deficiencies if a diet is consistently high in phytic acid-rich foods and low in mineral-rich foods. However, it's important to note that phytic acid also has antioxidant properties and may have health benefits when consumed as part of a balanced diet.

The bioavailability of minerals from phytic acid-rich foods can be improved through various methods such as soaking, sprouting, fermenting, or cooking, which can help break down some of the phytic acid and release the bound minerals.

Haptoglobins are proteins found in the blood that bind to free hemoglobin, which is released when red blood cells break down. The resulting complex is then removed from the bloodstream by the liver, preventing the loss of iron and potential kidney damage caused by the breakdown products of hemoglobin. Haptoglobins are produced in the liver and their levels can be measured to help diagnose various medical conditions such as hemolytic anemia, liver disease, and inflammation.

Blood protein electrophoresis (BPE) is a laboratory test that separates and measures the different proteins in the blood, such as albumin, alpha-1 globulins, alpha-2 globulins, beta globulins, and gamma globulins. This test is often used to help diagnose or monitor conditions related to abnormal protein levels, such as multiple myeloma, macroglobulinemia, and other plasma cell disorders.

In this test, a sample of the patient's blood is placed on a special gel and an electric current is applied. The proteins in the blood migrate through the gel based on their electrical charge and size, creating bands that can be visualized and measured. By comparing the band patterns to reference ranges, doctors can identify any abnormal protein levels or ratios, which may indicate underlying medical conditions.

It's important to note that while BPE is a useful diagnostic tool, it should be interpreted in conjunction with other clinical findings and laboratory tests for accurate diagnosis and management of the patient's condition.

Beta-thalassemia is a genetic blood disorder that affects the production of hemoglobin, a protein in red blood cells that carries oxygen throughout the body. Specifically, beta-thalassemia is caused by mutations in the beta-globin gene, which leads to reduced or absent production of the beta-globin component of hemoglobin.

There are two main types of beta-thalassemia:

1. Beta-thalassemia major (also known as Cooley's anemia): This is a severe form of the disorder that typically becomes apparent in early childhood. It is characterized by a significant reduction or absence of beta-globin production, leading to anemia, enlarged spleen and liver, jaundice, and growth retardation.
2. Beta-thalassemia intermedia: This is a milder form of the disorder that may not become apparent until later in childhood or even adulthood. It is characterized by a variable reduction in beta-globin production, leading to mild to moderate anemia and other symptoms that can range from nonexistent to severe.

Treatment for beta-thalassemia depends on the severity of the disorder and may include blood transfusions, iron chelation therapy, and/or bone marrow transplantation. In some cases, genetic counseling and prenatal diagnosis may also be recommended for families with a history of the disorder.

Sickle cell trait is a genetic condition where an individual inherits one abnormal gene for hemoglobin S (HbS) from one parent and one normal gene for hemoglobin A (HbA) from the other parent. Hemoglobin is a protein in red blood cells that carries oxygen throughout the body.

People with sickle cell trait do not have sickle cell disease, but they can pass the abnormal HbS gene on to their children. In certain situations, such as high altitude, low oxygen levels, or intense physical exertion, individuals with sickle cell trait may experience symptoms similar to those of sickle cell disease, such as fatigue, pain, and shortness of breath. However, these symptoms are typically milder and less frequent than in people with sickle cell disease.

It is important for individuals who know they have sickle cell trait to inform their healthcare providers, especially if they become pregnant or plan to engage in activities that may cause low oxygen levels, such as scuba diving or high-altitude climbing.

Hemoglobin M is a variant form of normal adult hemoglobin (Hb A) where the amino acid valine replaces the sulfur-containing amino acid, cysteine, at position 93 of the beta globin chain. This results in the formation of a stable bond between the heme iron and the globin protein, making it unable to release oxygen.

Hemoglobin M is not functional and causes a type of congenital hemolytic anemia that varies in severity depending on the specific mutation and the amount of Hemoglobin M present in the red blood cells. The condition can lead to chronic hypoxia, tissue damage, and other complications. It is inherited in an autosomal dominant manner, meaning only one copy of the altered gene from either parent is enough to cause the disorder.

Antisickling agents are medications or substances that help prevent or reduce the sickling of red blood cells in individuals with sickle cell disease. Sickling is a pathological process where the normally disc-shaped red blood cells become crescent-shaped due to abnormal hemoglobin (HbS). This change in shape can lead to blockages in small blood vessels, causing tissue damage and various complications such as pain crises, acute chest syndrome, and stroke.

Antisickling agents work by either inhibiting the polymerization of HbS or improving the oxygen-carrying capacity of red blood cells. The most commonly used antisickling agent is hydroxyurea, which increases the production of fetal hemoglobin (HbF) in red blood cells. HbF has a higher affinity for oxygen than HbS and can prevent the polymerization of HbS, thereby reducing sickling. Other antisickling agents include:

1. L-glutamine: An amino acid that helps maintain the structural integrity of red blood cells and reduces oxidative stress.
2. Arginate: A salt of arginine, an amino acid that helps improve nitric oxide production and vasodilation, reducing sickling.
3. Senicapoc: A drug that inhibits the formation of HbS polymers by blocking the interaction between HbS molecules.
4. Voxelotor (Oxbryta): A medication that binds to HbS and stabilizes it in its oxygenated state, reducing sickling.

These antisickling agents can help alleviate symptoms, decrease the frequency of pain crises, and improve the quality of life for individuals with sickle cell disease. However, they should be used under the supervision of a healthcare professional, as each has its benefits, risks, and potential side effects.

Alpha-thalassemia is a genetic disorder that affects the production of hemoglobin, a protein in red blood cells that carries oxygen throughout the body. It is caused by deletions or mutations in the genes that produce the alpha-globin chains of hemoglobin.

There are several types of alpha-thalassemia, ranging from mild to severe. The most severe form, called hydrops fetalis, occurs when all four alpha-globin genes are deleted or mutated. This can cause stillbirth or death shortly after birth due to heart failure and severe anemia.

Less severe forms of alpha-thalassemia can cause mild to moderate anemia, which may be asymptomatic or associated with symptoms such as fatigue, weakness, and jaundice. These forms of the disorder are more common in people from Mediterranean, Southeast Asian, and African backgrounds.

Treatment for alpha-thalassemia depends on the severity of the condition and may include blood transfusions, iron chelation therapy, or occasionally stem cell transplantation.

Ferritin is a protein in iron-metabolizing cells that stores iron in a water-soluble form. It is found inside the cells (intracellular) and is released into the bloodstream when the cells break down or die. Measuring the level of ferritin in the blood can help determine the amount of iron stored in the body. High levels of ferritin may indicate hemochromatosis, inflammation, liver disease, or other conditions. Low levels of ferritin may indicate anemia, iron deficiency, or other conditions.

Alpha-globins are a type of globin protein that combine to form the alpha-globin chains of hemoglobin, the oxygen-carrying protein in red blood cells. Hemoglobin is composed of four globin chains, two alpha-globin chains and two beta-globin chains, that surround a heme group. The alpha-globin genes are located on chromosome 16 and are essential for normal hemoglobin function. Mutations in the alpha-globin genes can lead to various forms of hemoglobin disorders such as alpha-thalassemia.

Abnormal erythrocytes refer to red blood cells that have an abnormal shape, size, or other characteristics. This can include various types of abnormalities such as:

1. Anisocytosis: Variation in the size of erythrocytes.
2. Poikilocytosis: Variation in the shape of erythrocytes, including but not limited to teardrop-shaped cells (dacrocytes), crescent-shaped cells (sickle cells), and spherical cells (spherocytes).
3. Anemia: A decrease in the total number of erythrocytes or a reduction in hemoglobin concentration, which can result from various underlying conditions such as iron deficiency, chronic disease, or blood loss.
4. Hemoglobinopathies: Abnormalities in the structure or function of hemoglobin, the protein responsible for carrying oxygen in erythrocytes, such as sickle cell anemia and thalassemia.
5. Inclusion bodies: Abnormal structures within erythrocytes, such as Heinz bodies (denatured hemoglobin) or Howell-Jolly bodies (nuclear remnants).

These abnormalities can be detected through a complete blood count (CBC) and peripheral blood smear examination. The presence of abnormal erythrocytes may indicate an underlying medical condition, and further evaluation is often necessary to determine the cause and appropriate treatment.

Myoglobin is a protein found in the muscle tissue, particularly in red or skeletal muscles. It belongs to the globin family and has a similar structure to hemoglobin, another oxygen-binding protein found in red blood cells. Myoglobin's primary function is to store oxygen within the muscle cells, making it readily available for use during periods of increased oxygen demand, such as during physical exertion.

Myoglobin contains heme groups that bind to and release oxygen molecules. The protein has a higher affinity for oxygen than hemoglobin, allowing it to maintain its bound oxygen even in low-oxygen environments. When muscle cells are damaged or undergo necrosis (cell death), myoglobin is released into the bloodstream and can be detected in serum or urine samples. Elevated levels of myoglobin in the blood or urine may indicate muscle injury, trauma, or diseases affecting muscle integrity, such as rhabdomyolysis or muscular dystrophies.

Hemolysis is the destruction or breakdown of red blood cells, resulting in the release of hemoglobin into the surrounding fluid (plasma). This process can occur due to various reasons such as chemical agents, infections, autoimmune disorders, mechanical trauma, or genetic abnormalities. Hemolysis may lead to anemia and jaundice, among other complications. It is essential to monitor hemolysis levels in patients undergoing medical treatments that might cause this condition.

Beta-globins are the type of globin proteins that make up the beta-chain of hemoglobin, the oxygen-carrying protein in red blood cells. Hemoglobin is composed of four polypeptide chains, two alpha-globin and two beta-globin chains, arranged in a specific structure. The beta-globin gene is located on chromosome 11, and mutations in this gene can lead to various forms of hemoglobin disorders such as sickle cell anemia and beta-thalassemia.

Hydrogen-ion concentration, also known as pH, is a measure of the acidity or basicity of a solution. It is defined as the negative logarithm (to the base 10) of the hydrogen ion activity in a solution. The standard unit of measurement is the pH unit. A pH of 7 is neutral, less than 7 is acidic, and greater than 7 is basic.

In medical terms, hydrogen-ion concentration is important for maintaining homeostasis within the body. For example, in the stomach, a high hydrogen-ion concentration (low pH) is necessary for the digestion of food. However, in other parts of the body such as blood, a high hydrogen-ion concentration can be harmful and lead to acidosis. Conversely, a low hydrogen-ion concentration (high pH) in the blood can lead to alkalosis. Both acidosis and alkalosis can have serious consequences on various organ systems if not corrected.

Hypochromic anemia is a type of anemia characterized by the presence of red blood cells that have lower than normal levels of hemoglobin and appear paler in color than normal. Hemoglobin is a protein in red blood cells that carries oxygen from the lungs to the rest of the body. In hypochromic anemia, there may be a decrease in the production or increased destruction of red blood cells, leading to a reduced number of red blood cells and insufficient oxygen supply to the tissues.

Hypochromic anemia can result from various underlying medical conditions, including iron deficiency, thalassemia, chronic inflammation, lead poisoning, and certain infections or chronic diseases. Treatment for hypochromic anemia depends on the underlying cause and may include iron supplements, dietary changes, medications, or blood transfusions.

Erythropoiesis is the process of forming and developing red blood cells (erythrocytes) in the body. It occurs in the bone marrow and is regulated by the hormone erythropoietin (EPO), which is produced by the kidneys. Erythropoiesis involves the differentiation and maturation of immature red blood cell precursors called erythroblasts into mature red blood cells, which are responsible for carrying oxygen to the body's tissues. Disorders that affect erythropoiesis can lead to anemia or other blood-related conditions.

Hemoglobinuria is a medical condition characterized by the presence of hemoglobin in the urine. Hemoglobin is a protein found in red blood cells that carries oxygen throughout the body. Normally, when red blood cells die, they are broken down and their hemoglobin is recycled. However, in certain conditions such as intravascular hemolysis (the destruction of red blood cells inside blood vessels), hemoglobin can be released into the bloodstream and then filtered by the kidneys into the urine.

Hemoglobinuria can be a symptom of various underlying medical conditions, including hemolytic anemias, disseminated intravascular coagulation (DIC), severe infections, snake bites, and exposure to certain toxins or medications. It is important to identify the underlying cause of hemoglobinuria, as treatment will depend on the specific condition.

In some cases, hemoglobinuria can lead to kidney damage due to the toxic effects of free hemoglobin on the renal tubules. This can result in acute or chronic kidney injury, and in severe cases, it may require dialysis or transplantation.

Polycythemia is a medical condition characterized by an abnormal increase in the total red blood cell (RBC) mass or hematocrit (the percentage of RBCs in the blood). This results in a higher-than-normal viscosity of the blood, which can lead to various complications such as impaired circulation, increased risk of blood clots, and reduced oxygen supply to the tissues.

There are two main types of polycythemia: primary and secondary. Primary polycythemia, also known as polycythemia vera, is a rare myeloproliferative neoplasm caused by genetic mutations that lead to excessive production of RBCs in the bone marrow. Secondary polycythemia, on the other hand, is a reactive condition triggered by various factors such as chronic hypoxia (low oxygen levels), high altitude, smoking, or certain medical conditions like sleep apnea, heart disease, or kidney tumors.

Symptoms of polycythemia may include fatigue, headaches, dizziness, shortness of breath, itching, and a bluish or reddish tint to the skin (cyanosis). Treatment depends on the underlying cause and severity of the condition and may involve phlebotomy, medications to reduce RBC production, and management of associated complications.

Hemin is defined as the iron(III) complex of protoporphyrin IX, which is a porphyrin derivative. It is a naturally occurring substance that is involved in various biological processes, most notably in the form of heme, which is a component of hemoglobin and other hemoproteins. Hemin is also used in medical research and therapy, such as in the treatment of methemoglobinemia and lead poisoning.

Spectrophotometry is a technical analytical method used in the field of medicine and science to measure the amount of light absorbed or transmitted by a substance at specific wavelengths. This technique involves the use of a spectrophotometer, an instrument that measures the intensity of light as it passes through a sample.

In medical applications, spectrophotometry is often used in laboratory settings to analyze various biological samples such as blood, urine, and tissues. For example, it can be used to measure the concentration of specific chemicals or compounds in a sample by measuring the amount of light that is absorbed or transmitted at specific wavelengths.

In addition, spectrophotometry can also be used to assess the properties of biological tissues, such as their optical density and thickness. This information can be useful in the diagnosis and treatment of various medical conditions, including skin disorders, eye diseases, and cancer.

Overall, spectrophotometry is a valuable tool for medical professionals and researchers seeking to understand the composition and properties of various biological samples and tissues.

Electrophoresis, cellulose acetate is a laboratory technique used to separate and analyze proteins or other charged molecules based on their size and charge. The sample is applied to a sheet of cellulose acetate, a type of porous plastic film, and an electric field is applied. The proteins migrate through the film towards the electrode with the opposite charge, with smaller and more negatively charged molecules moving faster than larger and less negatively charged ones. This allows for the separation and identification of different protein components in a mixture. It is a simple and rapid method for routine protein separations and is commonly used in biochemistry and molecular biology research.

Hematologic pregnancy complications refer to disorders related to the blood and blood-forming tissues that occur during pregnancy. These complications can have serious consequences for both the mother and the fetus if not properly managed. Some common hematologic pregnancy complications include:

1. Anemia: A condition characterized by a decrease in the number of red blood cells or hemoglobin in the blood, which can lead to fatigue, weakness, and shortness of breath. Iron-deficiency anemia is the most common type of anemia during pregnancy.
2. Thrombocytopenia: A condition characterized by a decrease in the number of platelets (cells that help blood clot) in the blood. Mild thrombocytopenia is relatively common during pregnancy, but severe thrombocytopenia can increase the risk of bleeding during delivery.
3. Gestational thrombotic thrombocytopenic purpura (GTTP): A rare but serious disorder that can cause blood clots to form in small blood vessels throughout the body, leading to a decrease in the number of platelets and red blood cells. GTTP can cause serious complications such as stroke, kidney failure, and even death if not promptly diagnosed and treated.
4. Disseminated intravascular coagulation (DIC): A condition characterized by abnormal clotting and bleeding throughout the body. DIC can be triggered by various conditions such as severe infections, pregnancy complications, or cancer.
5. Hemolysis, elevated liver enzymes, and low platelets (HELLP) syndrome: A serious complication of pregnancy that can cause damage to the liver and lead to bleeding. HELLP syndrome is often associated with preeclampsia, a condition characterized by high blood pressure and damage to organs such as the liver and kidneys.

It's important for pregnant women to receive regular prenatal care to monitor for these and other potential complications, and to seek prompt medical attention if any concerning symptoms arise.

Heinz bodies are small, irregularly shaped inclusions found in the red blood cells (RBCs). They are aggregates of denatured hemoglobin and are typically seen in RBCs that have been exposed to oxidative stress. This can occur due to various factors such as exposure to certain chemicals, drugs, or diseases.

The presence of Heinz bodies can lead to the premature destruction of RBCs, a condition known as hemolysis. This can result in anemia and related symptoms such as fatigue, weakness, and shortness of breath. It's important to note that while Heinz bodies are often associated with certain diseases, they can also be present in otherwise healthy individuals who have been exposed to oxidative stress.

It's worth mentioning that the term "Heinz bodies" comes from the name of the scientist Robert Heinz, who first described them in 1890.

An exchange transfusion of whole blood is a medical procedure in which a patient's blood is gradually replaced with donor whole blood. This procedure is typically performed in newborns or infants who have severe jaundice caused by excessive levels of bilirubin, a yellowish pigment that forms when hemoglobin from red blood cells breaks down.

During an exchange transfusion, the baby's blood is removed through a vein or artery and replaced with donor whole blood through another vein or artery. The process is repeated several times until a significant portion of the baby's blood has been exchanged with donor blood. This helps to reduce the levels of bilirubin in the baby's blood, which can help prevent or treat brain damage caused by excessive bilirubin.

Exchange transfusions are typically performed in a neonatal intensive care unit (NICU) and require close monitoring by a team of healthcare professionals. The procedure carries some risks, including infection, bleeding, and changes in blood pressure or heart rate. However, it can be a lifesaving treatment for newborns with severe jaundice who are at risk of developing serious complications.

Hematologic tests, also known as hematology tests, are a group of diagnostic exams that evaluate the health and function of different components of blood, such as red and white blood cells, platelets, and clotting factors. These tests can detect various disorders, including anemia, infection, bleeding problems, and several types of cancer. Common hematologic tests include complete blood count (CBC), coagulation studies, peripheral smear examination, and erythrocyte sedimentation rate (ESR). The specific test or combination of tests ordered will depend on the patient's symptoms, medical history, and physical examination findings.

Annelida is a phylum of bilaterally symmetrical, segmented animals that includes earthworms, leeches, and marine polychaetes (bristle worms). The name "Annelida" comes from the Latin word "annellus," meaning "little ring," which refers to the distinct segments found in these animals.

Each segment in annelids contains a pair of bundled nerves called the ventral nerve cord, and many also contain circular and longitudinal muscles that enable the animal to move by contracting and relaxing these muscles in a wave-like motion. Some annelids have specialized segments for functions such as reproduction or respiration.

Annelids are primarily aquatic animals, although some terrestrial species like earthworms have evolved to live on land. They vary in size from tiny marine worms that are only a few millimeters long to large marine polychaetes that can reach over a meter in length.

Annelids are important decomposers and help break down dead organic matter, returning nutrients to the soil or water. Some species of annelids are also parasitic, feeding on the blood or tissues of other animals. Overall, annelids play a crucial role in many aquatic and terrestrial ecosystems.

In the context of medicine and pharmacology, "kinetics" refers to the study of how a drug moves throughout the body, including its absorption, distribution, metabolism, and excretion (often abbreviated as ADME). This field is called "pharmacokinetics."

1. Absorption: This is the process of a drug moving from its site of administration into the bloodstream. Factors such as the route of administration (e.g., oral, intravenous, etc.), formulation, and individual physiological differences can affect absorption.

2. Distribution: Once a drug is in the bloodstream, it gets distributed throughout the body to various tissues and organs. This process is influenced by factors like blood flow, protein binding, and lipid solubility of the drug.

3. Metabolism: Drugs are often chemically modified in the body, typically in the liver, through processes known as metabolism. These changes can lead to the formation of active or inactive metabolites, which may then be further distributed, excreted, or undergo additional metabolic transformations.

4. Excretion: This is the process by which drugs and their metabolites are eliminated from the body, primarily through the kidneys (urine) and the liver (bile).

Understanding the kinetics of a drug is crucial for determining its optimal dosing regimen, potential interactions with other medications or foods, and any necessary adjustments for special populations like pediatric or geriatric patients, or those with impaired renal or hepatic function.

A reticulocyte count is a laboratory test that measures the percentage of reticulocytes in the peripheral blood. Reticulocytes are immature red blood cells produced in the bone marrow and released into the bloodstream. They contain residual ribosomal RNA, which gives them a reticular or net-like appearance under a microscope when stained with certain dyes.

The reticulocyte count is often used as an indicator of the rate of red blood cell production in the bone marrow. A higher than normal reticulocyte count may indicate an increased production of red blood cells, which can be seen in conditions such as hemolysis, blood loss, or response to treatment of anemia. A lower than normal reticulocyte count may suggest a decreased production of red blood cells, which can be seen in conditions such as bone marrow suppression, aplastic anemia, or vitamin deficiencies.

The reticulocyte count is usually expressed as a percentage of the total number of red blood cells, but it can also be reported as an absolute reticulocyte count (the actual number of reticulocytes per microliter of blood). The normal range for the reticulocyte count varies depending on the laboratory and the population studied.

I'm sorry for any confusion, but "Oligochaeta" is not a medical term. It is a taxonomic category in biology, specifically referring to a class of segmented worms, including earthworms and related species. They are characterized by having a simple circulatory system, and most have separate sexes. They are not directly relevant to human medical definition or healthcare context.

Heme proteins are a type of protein that contain a heme group, which is a prosthetic group composed of an iron atom contained in the center of a large organic ring called a porphyrin. The heme group gives these proteins their characteristic red color. Hemeproteins have various important functions in biological systems, including oxygen transport (e.g., hemoglobin), electron transfer (e.g., cytochromes), and enzymatic catalysis (e.g., peroxidases and catalases). The heme group can bind and release gases, such as oxygen and carbon monoxide, and can participate in redox reactions due to the ease with which iron can change its oxidation state.

Blood glucose, also known as blood sugar, is the concentration of glucose in the blood. Glucose is a simple sugar that serves as the main source of energy for the body's cells. It is carried to each cell through the bloodstream and is absorbed into the cells with the help of insulin, a hormone produced by the pancreas.

The normal range for blood glucose levels in humans is typically between 70 and 130 milligrams per deciliter (mg/dL) when fasting, and less than 180 mg/dL after meals. Levels that are consistently higher than this may indicate diabetes or other metabolic disorders.

Blood glucose levels can be measured through a variety of methods, including fingerstick blood tests, continuous glucose monitoring systems, and laboratory tests. Regular monitoring of blood glucose levels is important for people with diabetes to help manage their condition and prevent complications.

A blood transfusion is a medical procedure in which blood or its components are transferred from one individual (donor) to another (recipient) through a vein. The donated blood can be fresh whole blood, packed red blood cells, platelets, plasma, or cryoprecipitate, depending on the recipient's needs. Blood transfusions are performed to replace lost blood due to severe bleeding, treat anemia, support patients undergoing major surgeries, or manage various medical conditions such as hemophilia, thalassemia, and leukemia. The donated blood must be carefully cross-matched with the recipient's blood type to minimize the risk of transfusion reactions.

I must clarify that "Iron Isotopes" is not a medical term, but rather a scientific concept from the field of physics and chemistry. However, I can certainly provide a general explanation of isotopes and then focus on iron isotopes specifically.

An isotope is a variant of a chemical element that has the same number of protons (and thus the same atomic number) but a different number of neutrons within its nucleus. This results in variations of the atomic mass of isotopes of the same element. Some isotopes are stable, while others are unstable and will decay over time into other elements or isotopes, a process called radioactive decay.

Iron (Fe) has four naturally occurring stable isotopes: Fe-54, Fe-56, Fe-57, and Fe-58. These iron isotopes have different numbers of neutrons in their nuclei, resulting in slightly different atomic masses. The most abundant iron isotope is Fe-56, which contains 26 protons and 30 neutrons in its nucleus.

In the context of human health, iron is an essential nutrient that plays a crucial role in various biological processes, such as oxygen transport and energy production. However, the concept of iron isotopes does not have a direct medical relevance, but it can be useful in scientific research related to fields like geochemistry, environmental science, or nuclear physics.

Diabetes Mellitus is a chronic metabolic disorder characterized by elevated levels of glucose in the blood (hyperglycemia) due to absolute or relative deficiency in insulin secretion and/or insulin action. There are two main types: Type 1 diabetes, which results from the autoimmune destruction of pancreatic beta cells leading to insulin deficiency, and Type 2 diabetes, which is associated with insulin resistance and relative insulin deficiency.

Type 1 diabetes typically presents in childhood or young adulthood, while Type 2 diabetes tends to occur later in life, often in association with obesity and physical inactivity. Both types of diabetes can lead to long-term complications such as damage to the eyes, kidneys, nerves, and cardiovascular system if left untreated or not well controlled.

The diagnosis of diabetes is usually made based on fasting plasma glucose levels, oral glucose tolerance tests, or hemoglobin A1c (HbA1c) levels. Treatment typically involves lifestyle modifications such as diet and exercise, along with medications to lower blood glucose levels and manage associated conditions.

Near-infrared spectroscopy (NIRS) is a non-invasive optical technique that uses the near-infrared region of the electromagnetic spectrum (approximately 700-2500 nanometers) to analyze various chemical and physical properties of materials, primarily in the fields of biomedical research and industry. In medicine, NIRS is often used to measure tissue oxygenation, hemodynamics, and metabolism, providing valuable information about organ function and physiology. This technique is based on the principle that different molecules absorb and scatter near-infrared light differently, allowing for the identification and quantification of specific chromophores, such as oxyhemoglobin, deoxyhemoglobin, and cytochrome c oxidase. NIRS can be employed in a variety of clinical settings, including monitoring cerebral or muscle oxygenation during surgery, assessing tissue viability in wound healing, and studying brain function in neuroscience research.

Reticulocytes are immature red blood cells that still contain remnants of organelles, such as ribosomes and mitochondria, which are typically found in developing cells. These organelles are involved in the process of protein synthesis and energy production, respectively. Reticulocytes are released from the bone marrow into the bloodstream, where they continue to mature into fully developed red blood cells called erythrocytes.

Reticulocytes can be identified under a microscope by their staining characteristics, which reveal a network of fine filaments or granules known as the reticular apparatus. This apparatus is composed of residual ribosomal RNA and other proteins that have not yet been completely eliminated during the maturation process.

The percentage of reticulocytes in the blood can be used as a measure of bone marrow function and erythropoiesis, or red blood cell production. An increased reticulocyte count may indicate an appropriate response to blood loss, hemolysis, or other conditions that cause anemia, while a decreased count may suggest impaired bone marrow function or a deficiency in erythropoietin, the hormone responsible for stimulating red blood cell production.

Diabetes Mellitus, Type 2 is a metabolic disorder characterized by high blood glucose (or sugar) levels resulting from the body's inability to produce sufficient amounts of insulin or effectively use the insulin it produces. This form of diabetes usually develops gradually over several years and is often associated with older age, obesity, physical inactivity, family history of diabetes, and certain ethnicities.

In Type 2 diabetes, the body's cells become resistant to insulin, meaning they don't respond properly to the hormone. As a result, the pancreas produces more insulin to help glucose enter the cells. Over time, the pancreas can't keep up with the increased demand, leading to high blood glucose levels and diabetes.

Type 2 diabetes is managed through lifestyle modifications such as weight loss, regular exercise, and a healthy diet. Medications, including insulin therapy, may also be necessary to control blood glucose levels and prevent long-term complications associated with the disease, such as heart disease, nerve damage, kidney damage, and vision loss.

Fructosamine is a glycated protein that is formed when glucose binds to proteins in the bloodstream. It is used as an indicator of average blood glucose levels over the previous 2-3 weeks, and can be measured through a blood test. Fructosamine results are not affected by short-term changes in blood sugar levels or acute illnesses, making it useful for monitoring long-term glycemic control in people with diabetes.

The fructosamine test measures the level of glycated proteins in the blood, specifically those that have bound to serum albumin. The test results are reported as micromoles per liter (µmol/L) or millimoles per liter (mmol/L). Higher levels of fructosamine indicate poorer glucose control and an increased risk for diabetes complications, while lower levels suggest better glycemic control.

It's important to note that the fructosamine test is not a replacement for hemoglobin A1c (HbA1c) testing, which measures average blood glucose levels over the previous 2-3 months. Instead, it can be used as an additional tool in managing diabetes and assessing glycemic control.

Electrophoresis, starch gel is a type of electrophoretic technique used in laboratory settings for the separation and analysis of large biomolecules such as DNA, RNA, and proteins. In this method, a gel made from cooked starch is used as the supporting matrix for the molecules being separated.

The sample containing the mixture of biomolecules is loaded onto the gel and an electric field is applied, causing the negatively charged molecules to migrate towards the positive electrode. The starch gel acts as a molecular sieve, with smaller molecules moving more quickly through the gel than larger ones. This results in the separation of the mixture into individual components based on their size and charge.

Once the separation is complete, the gel can be stained to visualize the separated bands. Different staining techniques are used depending on the type of biomolecule being analyzed. For example, proteins can be stained with dyes such as Coomassie Brilliant Blue or silver nitrate, while nucleic acids can be stained with dyes such as ethidium bromide.

Starch gel electrophoresis is a relatively simple and inexpensive technique that has been widely used in molecular biology research and diagnostic applications. However, it has largely been replaced by other electrophoretic techniques, such as polyacrylamide gel electrophoresis (PAGE), which offer higher resolution and can be automated for high-throughput analysis.

Hemolytic anemia is a type of anemia that occurs when red blood cells are destroyed (hemolysis) faster than they can be produced. Red blood cells are essential for carrying oxygen throughout the body. When they are destroyed, hemoglobin and other cellular components are released into the bloodstream, which can lead to complications such as kidney damage and gallstones.

Hemolytic anemia can be inherited or acquired. Inherited forms of the condition may result from genetic defects that affect the structure or function of red blood cells. Acquired forms of hemolytic anemia can be caused by various factors, including infections, medications, autoimmune disorders, and certain medical conditions such as cancer or blood disorders.

Symptoms of hemolytic anemia may include fatigue, weakness, shortness of breath, pale skin, jaundice (yellowing of the skin and eyes), dark urine, and a rapid heartbeat. Treatment for hemolytic anemia depends on the underlying cause and may include medications, blood transfusions, or surgery.

Isoelectric focusing (IEF) is a technique used in electrophoresis, which is a method for separating proteins or other molecules based on their electrical charges. In IEF, a mixture of ampholytes (molecules that can carry both positive and negative charges) is used to create a pH gradient within a gel matrix. When an electric field is applied, the proteins or molecules migrate through the gel until they reach the point in the gradient where their net charge is zero, known as their isoelectric point (pI). At this point, they focus into a sharp band and stop moving, resulting in a highly resolved separation of the different components based on their pI. This technique is widely used in protein research for applications such as protein identification, characterization, and purification.

Hemoglobin is a complex protein in red blood cells that consists of four polypeptide chains, two alpha (α) and two beta (β) subunits. Each subunit can bind to a heme group, which contains an iron atom that facilitates the binding and transportation of oxygen from the lungs to the body's tissues.

The terms 'hemoglobin subunits' or 'hemoglobin components' typically refer to these individual polypeptide chains: alpha, beta, gamma (γ), delta (δ), epsilon (ε), and zeta (ζ) subunits. The different types of hemoglobin found in humans are primarily distinguished by the specific combination of these subunits.

- Hemoglobin A (HbA): This is the most common adult hemoglobin, consisting of two alpha and two beta subunits (α2β2).
- Hemoglobin A2 (HbA2): This is a minor adult hemoglobin, comprising about 1.5% to 3.5% of total hemoglobin in adults. It contains two alpha and two delta subunits (α2δ2).
- Hemoglobin F (HbF): This fetal hemoglobin consists of two alpha and two gamma subunits (α2γ2) and is the primary form of hemoglobin in a developing fetus. After birth, HbF levels decrease as HbA becomes the dominant type.
- Hemoglobin A1c (HbA1c): This is not a distinct hemoglobin subunit but rather a glycated form of hemoglobin A, where glucose binds to the beta subunits. HbA1c levels are used as a diagnostic marker for average blood sugar levels over the previous 2-3 months in people with diabetes mellitus.

In summary, 'hemoglobin subunits' refer to the individual polypeptide chains that make up hemoglobin molecules, including alpha, beta, gamma, delta, epsilon, and zeta subunits. Different combinations of these subunits form distinct types of hemoglobins, such as HbA, HbF, and HbA1c.

Photolysis is a term used in medical and scientific contexts to describe a chemical reaction that is initiated by the absorption of light or photons. In this process, a molecule absorbs a photon, which provides sufficient energy to break a bond within the molecule, leading to the formation of two or more smaller molecules or radicals. This phenomenon is particularly relevant in fields such as pharmacology and toxicology, where photolysis can alter the chemical structure and biological activity of drugs and other substances upon exposure to light.

Macromolecular substances, also known as macromolecules, are large, complex molecules made up of repeating subunits called monomers. These substances are formed through polymerization, a process in which many small molecules combine to form a larger one. Macromolecular substances can be naturally occurring, such as proteins, DNA, and carbohydrates, or synthetic, such as plastics and synthetic fibers.

In the context of medicine, macromolecular substances are often used in the development of drugs and medical devices. For example, some drugs are designed to bind to specific macromolecules in the body, such as proteins or DNA, in order to alter their function and produce a therapeutic effect. Additionally, macromolecular substances may be used in the creation of medical implants, such as artificial joints and heart valves, due to their strength and durability.

It is important for healthcare professionals to have an understanding of macromolecular substances and how they function in the body, as this knowledge can inform the development and use of medical treatments.

A "Blood Cell Count" is a medical laboratory test that measures the number of red blood cells (RBCs), white blood cells (WBCs), and platelets in a sample of blood. This test is often used as a part of a routine check-up or to help diagnose various medical conditions, such as anemia, infection, inflammation, and many others.

The RBC count measures the number of oxygen-carrying cells in the blood, while the WBC count measures the number of immune cells that help fight infections. The platelet count measures the number of cells involved in clotting. Abnormal results in any of these counts may indicate an underlying medical condition and further testing may be required for diagnosis and treatment.

Protein conformation refers to the specific three-dimensional shape that a protein molecule assumes due to the spatial arrangement of its constituent amino acid residues and their associated chemical groups. This complex structure is determined by several factors, including covalent bonds (disulfide bridges), hydrogen bonds, van der Waals forces, and ionic bonds, which help stabilize the protein's unique conformation.

Protein conformations can be broadly classified into two categories: primary, secondary, tertiary, and quaternary structures. The primary structure represents the linear sequence of amino acids in a polypeptide chain. The secondary structure arises from local interactions between adjacent amino acid residues, leading to the formation of recurring motifs such as α-helices and β-sheets. Tertiary structure refers to the overall three-dimensional folding pattern of a single polypeptide chain, while quaternary structure describes the spatial arrangement of multiple folded polypeptide chains (subunits) that interact to form a functional protein complex.

Understanding protein conformation is crucial for elucidating protein function, as the specific three-dimensional shape of a protein directly influences its ability to interact with other molecules, such as ligands, nucleic acids, or other proteins. Any alterations in protein conformation due to genetic mutations, environmental factors, or chemical modifications can lead to loss of function, misfolding, aggregation, and disease states like neurodegenerative disorders and cancer.

In the field of medicine, "time factors" refer to the duration of symptoms or time elapsed since the onset of a medical condition, which can have significant implications for diagnosis and treatment. Understanding time factors is crucial in determining the progression of a disease, evaluating the effectiveness of treatments, and making critical decisions regarding patient care.

For example, in stroke management, "time is brain," meaning that rapid intervention within a specific time frame (usually within 4.5 hours) is essential to administering tissue plasminogen activator (tPA), a clot-busting drug that can minimize brain damage and improve patient outcomes. Similarly, in trauma care, the "golden hour" concept emphasizes the importance of providing definitive care within the first 60 minutes after injury to increase survival rates and reduce morbidity.

Time factors also play a role in monitoring the progression of chronic conditions like diabetes or heart disease, where regular follow-ups and assessments help determine appropriate treatment adjustments and prevent complications. In infectious diseases, time factors are crucial for initiating antibiotic therapy and identifying potential outbreaks to control their spread.

Overall, "time factors" encompass the significance of recognizing and acting promptly in various medical scenarios to optimize patient outcomes and provide effective care.

An erythrocyte transfusion, also known as a red blood cell (RBC) transfusion, is the process of transferring compatible red blood cells from a donor to a recipient. This procedure is typically performed to increase the recipient's oxygen-carrying capacity, usually in situations where there is significant blood loss, anemia, or impaired red blood cell production.

During the transfusion, the donor's red blood cells are collected, typed, and tested for compatibility with the recipient's blood to minimize the risk of a transfusion reaction. Once compatible units are identified, they are infused into the recipient's circulation through a sterile intravenous (IV) line. The recipient's body will eventually eliminate the donated red blood cells within 100-120 days as part of its normal turnover process.

Erythrocyte transfusions can be lifesaving in various clinical scenarios, such as trauma, surgery, severe anemia due to chronic diseases, and hematologic disorders. However, they should only be used when necessary, as there are potential risks associated with the procedure, including allergic reactions, transmission of infectious diseases, transfusion-related acute lung injury (TRALI), and iron overload in cases of multiple transfusions.

Protein binding, in the context of medical and biological sciences, refers to the interaction between a protein and another molecule (known as the ligand) that results in a stable complex. This process is often reversible and can be influenced by various factors such as pH, temperature, and concentration of the involved molecules.

In clinical chemistry, protein binding is particularly important when it comes to drugs, as many of them bind to proteins (especially albumin) in the bloodstream. The degree of protein binding can affect a drug's distribution, metabolism, and excretion, which in turn influence its therapeutic effectiveness and potential side effects.

Protein-bound drugs may be less available for interaction with their target tissues, as only the unbound or "free" fraction of the drug is active. Therefore, understanding protein binding can help optimize dosing regimens and minimize adverse reactions.

Ferrous compounds are inorganic substances that contain iron (Fe) in its +2 oxidation state. The term "ferrous" is derived from the Latin word "ferrum," which means iron. Ferrous compounds are often used in medicine, particularly in the treatment of iron-deficiency anemia due to their ability to provide bioavailable iron to the body.

Examples of ferrous compounds include ferrous sulfate, ferrous gluconate, and ferrous fumarate. These compounds are commonly found in dietary supplements and multivitamins. Ferrous sulfate is one of the most commonly used forms of iron supplementation, as it has a high iron content and is relatively inexpensive.

It's important to note that ferrous compounds can be toxic in large doses, so they should be taken under the guidance of a healthcare professional. Overdose can lead to symptoms such as nausea, vomiting, diarrhea, abdominal pain, and potentially fatal consequences if left untreated.

Allosteric regulation is a process that describes the way in which the binding of a molecule (known as a ligand) to an enzyme or protein at one site affects the ability of another molecule to bind to a different site on the same enzyme or protein. This interaction can either enhance (positive allosteric regulation) or inhibit (negative allosteric regulation) the activity of the enzyme or protein, depending on the nature of the ligand and its effect on the shape and/or conformation of the enzyme or protein.

In an allosteric regulatory system, the binding of the first molecule to the enzyme or protein causes a conformational change in the protein structure that alters the affinity of the second site for its ligand. This can result in changes in the activity of the enzyme or protein, allowing for fine-tuning of biochemical pathways and regulatory processes within cells.

Allosteric regulation is a fundamental mechanism in many biological systems, including metabolic pathways, signal transduction cascades, and gene expression networks. Understanding allosteric regulation can provide valuable insights into the mechanisms underlying various physiological and pathological processes, and can inform the development of novel therapeutic strategies for the treatment of disease.

Renal dialysis is a medical procedure that is used to artificially remove waste products, toxins, and excess fluids from the blood when the kidneys are no longer able to perform these functions effectively. This process is also known as hemodialysis.

During renal dialysis, the patient's blood is circulated through a special machine called a dialyzer or an artificial kidney, which contains a semi-permeable membrane that filters out waste products and excess fluids from the blood. The cleaned blood is then returned to the patient's body.

Renal dialysis is typically recommended for patients with advanced kidney disease or kidney failure, such as those with end-stage renal disease (ESRD). It is a life-sustaining treatment that helps to maintain the balance of fluids and electrolytes in the body, prevent the buildup of waste products and toxins, and control blood pressure.

There are two main types of renal dialysis: hemodialysis and peritoneal dialysis. Hemodialysis is the most common type and involves using a dialyzer to filter the blood outside the body. Peritoneal dialysis, on the other hand, involves placing a catheter in the abdomen and using the lining of the abdomen (peritoneum) as a natural filter to remove waste products and excess fluids from the body.

Overall, renal dialysis is an essential treatment option for patients with kidney failure, helping them to maintain their quality of life and prolong their survival.

High-performance liquid chromatography (HPLC) is a type of chromatography that separates and analyzes compounds based on their interactions with a stationary phase and a mobile phase under high pressure. The mobile phase, which can be a gas or liquid, carries the sample mixture through a column containing the stationary phase.

In HPLC, the mobile phase is a liquid, and it is pumped through the column at high pressures (up to several hundred atmospheres) to achieve faster separation times and better resolution than other types of liquid chromatography. The stationary phase can be a solid or a liquid supported on a solid, and it interacts differently with each component in the sample mixture, causing them to separate as they travel through the column.

HPLC is widely used in analytical chemistry, pharmaceuticals, biotechnology, and other fields to separate, identify, and quantify compounds present in complex mixtures. It can be used to analyze a wide range of substances, including drugs, hormones, vitamins, pigments, flavors, and pollutants. HPLC is also used in the preparation of pure samples for further study or use.

I apologize for any confusion, but "Vitreoscilla" is not a medical term. It is actually the name of a genus of bacteria that are commonly found in soil and water. The bacteria are known for their ability to survive under low oxygen conditions. They have a unique characteristic of being able to switch between aerobic and anaerobic metabolism, which makes them interesting for research purposes.

If you have any questions related to medical terminology or health-related topics, I would be happy to help with those instead!

Erythrocyte volume, also known as red cell volume or hematocrit, is the proportion of whole blood that is made up of erythrocytes or red blood cells. It is typically expressed as a percentage and can be measured using a centrifuge to separate the components of a blood sample by density.

The erythrocyte volume is an important clinical parameter because it can provide information about a person's health status, such as their hydration level, altitude acclimatization, and the presence of certain medical conditions like anemia or polycythemia. Changes in erythrocyte volume can also have significant effects on the body's oxygen-carrying capacity and overall cardiovascular function.

Erythrocyte aging, also known as red cell aging, is the natural process of changes and senescence that occur in red blood cells (erythrocytes) over time. In humans, mature erythrocytes are devoid of nuclei and organelles, and have a lifespan of approximately 120 days.

During aging, several biochemical and structural modifications take place in the erythrocyte, including:

1. Loss of membrane phospholipids and proteins, leading to increased rigidity and decreased deformability.
2. Oxidative damage to hemoglobin, resulting in the formation of methemoglobin and heinz bodies.
3. Accumulation of denatured proteins and aggregates, which can impair cellular functions.
4. Changes in the cytoskeleton, affecting the shape and stability of the erythrocyte.
5. Increased expression of surface markers, such as Band 3 and CD47, that signal the spleen to remove aged erythrocytes from circulation.

The spleen plays a crucial role in removing senescent erythrocytes by recognizing and phagocytosing those with altered membrane composition or increased expression of surface markers. This process helps maintain the overall health and functionality of the circulatory system.

In the context of medicine, and specifically in physiology and respiratory therapy, partial pressure (P or p) is a measure of the pressure exerted by an individual gas in a mixture of gases. It's commonly used to describe the concentrations of gases in the body, such as oxygen (PO2), carbon dioxide (PCO2), and nitrogen (PN2).

The partial pressure of a specific gas is calculated as the fraction of that gas in the total mixture multiplied by the total pressure of the mixture. This concept is based on Dalton's law, which states that the total pressure exerted by a mixture of gases is equal to the sum of the pressures exerted by each individual gas.

For example, in room air at sea level, the partial pressure of oxygen (PO2) is approximately 160 mmHg (mm of mercury), which represents about 21% of the total barometric pressure (760 mmHg). This concept is crucial for understanding gas exchange in the lungs and how gases move across membranes, such as from alveoli to blood and vice versa.

I'm sorry for any confusion, but "Polychaeta" is not a medical term. It is a taxonomic category in zoology, specifically referring to a class of annelid worms commonly known as bristle worms or polychaetes. These are segmented worms that have pairs of fleshy protrusions called parapodia on most or all segments, which they use for locomotion. Some species live in marine environments, while others can be found in fresh water or even terrestrial habitats. If you have a medical term you would like me to define, I'd be happy to help!

Hemodilution is a medical term that refers to the reduction in the concentration of certain components in the blood, usually referring to red blood cells (RBCs) or hemoglobin. This occurs when an individual's plasma volume expands due to the infusion of intravenous fluids or the body's own production of fluid, such as during severe infection or inflammation. As a result, the number of RBCs per unit of blood decreases, leading to a lower hematocrit and hemoglobin level. It is important to note that while hemodilution reduces the concentration of RBCs in the blood, it does not necessarily indicate anemia or blood loss.

Oxidation-Reduction (redox) reactions are a type of chemical reaction involving a transfer of electrons between two species. The substance that loses electrons in the reaction is oxidized, and the substance that gains electrons is reduced. Oxidation and reduction always occur together in a redox reaction, hence the term "oxidation-reduction."

In biological systems, redox reactions play a crucial role in many cellular processes, including energy production, metabolism, and signaling. The transfer of electrons in these reactions is often facilitated by specialized molecules called electron carriers, such as nicotinamide adenine dinucleotide (NAD+/NADH) and flavin adenine dinucleotide (FAD/FADH2).

The oxidation state of an element in a compound is a measure of the number of electrons that have been gained or lost relative to its neutral state. In redox reactions, the oxidation state of one or more elements changes as they gain or lose electrons. The substance that is oxidized has a higher oxidation state, while the substance that is reduced has a lower oxidation state.

Overall, oxidation-reduction reactions are fundamental to the functioning of living organisms and are involved in many important biological processes.

Bivalvia is a class of mollusks, also known as "pelecypods," that have a laterally compressed body and two shells or valves. These valves are hinged together on one side and can be opened and closed to allow the animal to feed or withdraw into its shell for protection.

Bivalves include clams, oysters, mussels, scallops, and numerous other species. They are characterized by their simple body structure, which consists of a muscular foot used for burrowing or anchoring, a soft mantle that secretes the shell, and gills that serve both as respiratory organs and feeding structures.

Bivalves play an important role in aquatic ecosystems as filter feeders, helping to maintain water quality by removing particles and organic matter from the water column. They are also commercially important as a source of food for humans and other animals, and their shells have been used historically for various purposes such as tools, jewelry, and building materials.

Recombinant proteins are artificially created proteins produced through the use of recombinant DNA technology. This process involves combining DNA molecules from different sources to create a new set of genes that encode for a specific protein. The resulting recombinant protein can then be expressed, purified, and used for various applications in research, medicine, and industry.

Recombinant proteins are widely used in biomedical research to study protein function, structure, and interactions. They are also used in the development of diagnostic tests, vaccines, and therapeutic drugs. For example, recombinant insulin is a common treatment for diabetes, while recombinant human growth hormone is used to treat growth disorders.

The production of recombinant proteins typically involves the use of host cells, such as bacteria, yeast, or mammalian cells, which are engineered to express the desired protein. The host cells are transformed with a plasmid vector containing the gene of interest, along with regulatory elements that control its expression. Once the host cells are cultured and the protein is expressed, it can be purified using various chromatography techniques.

Overall, recombinant proteins have revolutionized many areas of biology and medicine, enabling researchers to study and manipulate proteins in ways that were previously impossible.

Pallor is a medical term that refers to an abnormal pale appearance of the skin, mucous membranes, or nail beds. It can be a sign of various underlying medical conditions such as anemia (a decrease in red blood cells or hemoglobin), blood loss, malnutrition, vitamin deficiencies, or certain diseases that affect circulation or oxygenation of the blood. Pallor can also occur due to emotional distress or fear, leading to a temporary reduction in blood flow to the skin. It is important to note that pallor should be evaluated in conjunction with other symptoms and medical history for an accurate diagnosis.

Chironomidae is a family of nematoceran flies, also known as non-biting midges or lake flies. They are often mistaken for mosquitoes due to their similar appearance, but they do not bite and are not vectors for disease. Chironomidae species can be found in various aquatic habitats such as lakes, rivers, and wetlands. The larvae of these flies are an important food source for many fish and other aquatic organisms. Adult chironomids are also known to emerge in large numbers in a synchronized fashion, particularly near bodies of water, which can be a nuisance to nearby human populations.

Gamma-globulins are a type of globulin, which are proteins found in the blood plasma. More specifically, gamma-globulins are a class of immunoglobulins, also known as antibodies, that play a crucial role in the immune system's response to foreign substances and infectious agents.

Immunoglobulins are divided into several classes based on their structure and function. Gamma-globulins include IgG, IgA, and IgD isotypes of immunoglobulins. Among these, IgG is the most abundant type found in the blood and other body fluids, responsible for providing protection against bacterial and viral infections.

Gamma-globulins are produced by B cells, a type of white blood cell involved in the immune response. They can be measured in the blood as part of a complete blood count (CBC) or specific protein electrophoresis tests to assess immune system function or diagnose various medical conditions such as infections, inflammation, and autoimmune disorders.

Pulse oximetry is a noninvasive method for monitoring a person's oxygen saturation (SO2) and pulse rate. It uses a device called a pulse oximeter, which measures the amount of oxygen-carrying hemoglobin in the blood compared to the amount of hemoglobin that is not carrying oxygen. This measurement is expressed as a percentage, known as oxygen saturation (SpO2). Normal oxygen saturation levels are generally 95% or above at sea level. Lower levels may indicate hypoxemia, a condition where there is not enough oxygen in the blood to meet the body's needs. Pulse oximetry is commonly used in hospitals and other healthcare settings to monitor patients during surgery, in intensive care units, and in sleep studies to detect conditions such as sleep apnea. It can also be used by individuals with certain medical conditions, such as chronic obstructive pulmonary disease (COPD), to monitor their oxygen levels at home.

Phenylhydrazines are organic compounds that contain a phenyl group (a benzene ring with a hydrogen atom substituted by a hydroxy group) and a hydrazine group (-NH-NH2). They are aromatic amines that have been used in various chemical reactions, including the formation of azos and hydrazones. In medicine, phenylhydrazines were once used as vasodilators to treat angina pectoris, but their use has largely been discontinued due to their toxicity and potential carcinogenicity.

Sulfhemoglobin is a dark blue, chemically stable form of hemoglobin that results from the reaction between hemoglobin and sulfur-containing compounds such as sulfide or certain drugs like phenacetin. It has a limited ability to transport oxygen, leading to potential hypoxia if it accumulates in high concentrations. Sulfhemoglobinemia is the condition characterized by an increased level of sulfhemoglobin in the blood.

Chronic kidney failure, also known as chronic kidney disease (CKD) stage 5 or end-stage renal disease (ESRD), is a permanent loss of kidney function that occurs gradually over a period of months to years. It is defined as a glomerular filtration rate (GFR) of less than 15 ml/min, which means the kidneys are filtering waste and excess fluids at less than 15% of their normal capacity.

CKD can be caused by various underlying conditions such as diabetes, hypertension, glomerulonephritis, polycystic kidney disease, and recurrent kidney infections. Over time, the damage to the kidneys can lead to a buildup of waste products and fluids in the body, which can cause a range of symptoms including fatigue, weakness, shortness of breath, nausea, vomiting, and confusion.

Treatment for chronic kidney failure typically involves managing the underlying condition, making lifestyle changes such as following a healthy diet, and receiving supportive care such as dialysis or a kidney transplant to replace lost kidney function.

Nitric oxide (NO) is a molecule made up of one nitrogen atom and one oxygen atom. In the body, it is a crucial signaling molecule involved in various physiological processes such as vasodilation, immune response, neurotransmission, and inhibition of platelet aggregation. It is produced naturally by the enzyme nitric oxide synthase (NOS) from the amino acid L-arginine. Inhaled nitric oxide is used medically to treat pulmonary hypertension in newborns and adults, as it helps to relax and widen blood vessels, improving oxygenation and blood flow.

Hydroxyurea is an antimetabolite drug that is primarily used in the treatment of myeloproliferative disorders such as chronic myelogenous leukemia (CML), essential thrombocythemia, and polycythemia vera. It works by interfering with the synthesis of DNA, which inhibits the growth of cancer cells.

In addition to its use in cancer therapy, hydroxyurea is also used off-label for the management of sickle cell disease. In this context, it helps to reduce the frequency and severity of painful vaso-occlusive crises by increasing the production of fetal hemoglobin (HbF), which decreases the formation of sickled red blood cells.

The medical definition of hydroxyurea is:

A hydantoin derivative and antimetabolite that inhibits ribonucleoside diphosphate reductase, thereby interfering with DNA synthesis. It has been used as an antineoplastic agent, particularly in the treatment of myeloproliferative disorders, and more recently for the management of sickle cell disease to reduce the frequency and severity of painful vaso-occlusive crises by increasing fetal hemoglobin production.

Dietary iron is a vital nutrient that plays a crucial role in the production of hemoglobin, a protein in red blood cells responsible for carrying oxygen throughout the body. It is also essential for various other bodily functions, including energy production and immune function.

There are two forms of dietary iron: heme and non-heme. Heme iron is found in animal products such as meat, poultry, and fish, while non-heme iron is found in plant-based foods such as beans, lentils, tofu, spinach, and fortified cereals.

The recommended daily intake of dietary iron varies depending on age, sex, and other factors. For example, adult men typically require 8 milligrams (mg) per day, while adult women need 18 mg per day. Pregnant women may require up to 27 mg per day, while breastfeeding women need around 9-10 mg per day.

It is important to note that the absorption of non-heme iron from plant-based foods can be enhanced by consuming them with vitamin C-rich foods or drinks, such as citrus fruits, strawberries, and bell peppers. On the other hand, certain substances such as tannins (found in tea and coffee) and phytates (found in whole grains and legumes) can inhibit the absorption of non-heme iron.

Protoporphyrins are organic compounds that are the immediate precursors to heme in the porphyrin synthesis pathway. They are composed of a porphyrin ring, which is a large, complex ring made up of four pyrrole rings joined together, with an acetate and a propionate side chain at each pyrrole. Protoporphyrins are commonly found in nature and are important components of many biological systems, including hemoglobin, the protein in red blood cells that carries oxygen throughout the body.

There are several different types of protoporphyrins, including protoporphyrin IX, which is the most common form found in humans and other animals. Protoporphyrins can be measured in the blood or other tissues as a way to diagnose or monitor certain medical conditions, such as lead poisoning or porphyrias, which are rare genetic disorders that affect the production of heme. Elevated levels of protoporphyrins in the blood or tissues can indicate the presence of these conditions and may require further evaluation and treatment.

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.

Spectrum analysis in the context of Raman spectroscopy refers to the measurement and interpretation of the Raman scattering spectrum of a material or sample. Raman spectroscopy is a non-destructive analytical technique that uses the inelastic scattering of light to examine the vibrational modes of molecules.

When a monochromatic light source, typically a laser, illuminates a sample, a small fraction of the scattered light undergoes a shift in frequency due to interactions with the molecular vibrations of the sample. This shift in frequency is known as the Raman shift and is unique to each chemical bond or functional group within a molecule.

In a Raman spectrum, the intensity of the scattered light is plotted against the Raman shift, which is expressed in wavenumbers (cm-1). The resulting spectrum provides a "fingerprint" of the sample's molecular structure and composition, allowing for the identification and characterization of various chemical components within the sample.

Spectrum analysis in Raman spectroscopy can reveal valuable information about the sample's crystallinity, phase transitions, polymorphism, molecular orientation, and other properties. This technique is widely used across various fields, including materials science, chemistry, biology, pharmaceuticals, and forensics, to analyze a diverse range of samples, from simple liquids and solids to complex biological tissues and nanomaterials.

Blood chemical analysis, also known as clinical chemistry or chemistry panel, is a series of tests that measure the levels of various chemicals in the blood. These tests can help evaluate the function of organs such as the kidneys and liver, and can also detect conditions such as diabetes and heart disease.

The tests typically include:

* Glucose: to check for diabetes
* Electrolytes (such as sodium, potassium, chloride, and bicarbonate): to check the body's fluid and electrolyte balance
* Calcium: to check for problems with bones, nerves, or kidneys
* Creatinine: to check for kidney function
* Urea Nitrogen (BUN): to check for kidney function
* Albumin: to check for liver function and nutrition status
* ALT (Alanine Transaminase) and AST (Aspartate Transaminase): to check for liver function
* Alkaline Phosphatase: to check for liver or bone disease
* Total Bilirubin: to check for liver function and gallbladder function
* Cholesterol: to check for heart disease risk
* Triglycerides: to check for heart disease risk

These tests are usually ordered by a doctor as part of a routine check-up, or to help diagnose and monitor specific medical conditions. The results of the blood chemical analysis are compared to reference ranges provided by the laboratory performing the test, which take into account factors such as age, sex, and race.

An erythrocyte, also known as a red blood cell, is a type of cell that circulates in the blood and is responsible for transporting oxygen throughout the body. The erythrocyte membrane refers to the thin, flexible barrier that surrounds the erythrocyte and helps to maintain its shape and stability.

The erythrocyte membrane is composed of a lipid bilayer, which contains various proteins and carbohydrates. These components help to regulate the movement of molecules into and out of the erythrocyte, as well as provide structural support and protection for the cell.

The main lipids found in the erythrocyte membrane are phospholipids and cholesterol, which are arranged in a bilayer structure with the hydrophilic (water-loving) heads facing outward and the hydrophobic (water-fearing) tails facing inward. This arrangement helps to maintain the integrity of the membrane and prevent the leakage of cellular components.

The proteins found in the erythrocyte membrane include integral proteins, which span the entire width of the membrane, and peripheral proteins, which are attached to the inner or outer surface of the membrane. These proteins play a variety of roles, such as transporting molecules across the membrane, maintaining the shape of the erythrocyte, and interacting with other cells and proteins in the body.

The carbohydrates found in the erythrocyte membrane are attached to the outer surface of the membrane and help to identify the cell as part of the body's own immune system. They also play a role in cell-cell recognition and adhesion.

Overall, the erythrocyte membrane is a complex and dynamic structure that plays a critical role in maintaining the function and integrity of red blood cells.

Erythrocruorins are large, oxygen-carrying protein molecules found in the blood of certain annelid worms and some arthropods. They function similarly to hemoglobin in vertebrates, binding to oxygen and facilitating its transport throughout the body. Erythrocruorins are composed of multiple subunits, creating a complex structure that enhances their oxygen-binding capacity. The term 'erythrocruorin' comes from the Greek words "erythros," meaning red, and "cruor," meaning blood.

Treatment outcome is a term used to describe the result or effect of medical treatment on a patient's health status. It can be measured in various ways, such as through symptoms improvement, disease remission, reduced disability, improved quality of life, or survival rates. The treatment outcome helps healthcare providers evaluate the effectiveness of a particular treatment plan and make informed decisions about future care. It is also used in clinical research to compare the efficacy of different treatments and improve patient care.

I'm sorry for any confusion, but "spectrum analysis" is not a commonly used medical term. Spectrum analysis is a term that is more frequently used in the fields of physics, mathematics, and engineering to describe the process of breaking down a signal or a wave into its different frequencies and amplitudes, creating a visual representation called a spectrum.

If you have any concerns about a medical issue, I would recommend consulting with a healthcare professional for accurate information and guidance.

Mercuribenzoates are organic compounds that contain a mercury atom bonded to a benzoate group. They were historically used as diuretics and antiseptics, but their use has been largely discontinued due to the toxicity of mercury.

The medical definition of Mercuribenzoates is not widely used in modern medicine, as these compounds have fallen out of favor due to safer and more effective treatment options being available. Additionally, the use of mercury-containing compounds in medicine has become increasingly restricted due to concerns about their environmental impact and potential health risks.

Prospective studies, also known as longitudinal studies, are a type of cohort study in which data is collected forward in time, following a group of individuals who share a common characteristic or exposure over a period of time. The researchers clearly define the study population and exposure of interest at the beginning of the study and follow up with the participants to determine the outcomes that develop over time. This type of study design allows for the investigation of causal relationships between exposures and outcomes, as well as the identification of risk factors and the estimation of disease incidence rates. Prospective studies are particularly useful in epidemiology and medical research when studying diseases with long latency periods or rare outcomes.

A biological marker, often referred to as a biomarker, is a measurable indicator that reflects the presence or severity of a disease state, or a response to a therapeutic intervention. Biomarkers can be found in various materials such as blood, tissues, or bodily fluids, and they can take many forms, including molecular, histologic, radiographic, or physiological measurements.

In the context of medical research and clinical practice, biomarkers are used for a variety of purposes, such as:

1. Diagnosis: Biomarkers can help diagnose a disease by indicating the presence or absence of a particular condition. For example, prostate-specific antigen (PSA) is a biomarker used to detect prostate cancer.
2. Monitoring: Biomarkers can be used to monitor the progression or regression of a disease over time. For instance, hemoglobin A1c (HbA1c) levels are monitored in diabetes patients to assess long-term blood glucose control.
3. Predicting: Biomarkers can help predict the likelihood of developing a particular disease or the risk of a negative outcome. For example, the presence of certain genetic mutations can indicate an increased risk for breast cancer.
4. Response to treatment: Biomarkers can be used to evaluate the effectiveness of a specific treatment by measuring changes in the biomarker levels before and after the intervention. This is particularly useful in personalized medicine, where treatments are tailored to individual patients based on their unique biomarker profiles.

It's important to note that for a biomarker to be considered clinically valid and useful, it must undergo rigorous validation through well-designed studies, including demonstrating sensitivity, specificity, reproducibility, and clinical relevance.

I believe there may be some confusion in your question. Whales are not a medical term but rather large marine mammals. They belong to the Cetacean family, which includes dolphins and porpoises. If you're asking about a medical condition or something similar that might be associated with the word "whales," I would need more information to provide an accurate response.

Ion exchange chromatography is a type of chromatography technique used to separate and analyze charged molecules (ions) based on their ability to exchange bound ions in a solid resin or gel with ions of similar charge in the mobile phase. The stationary phase, often called an ion exchanger, contains fixed ated functional groups that can attract counter-ions of opposite charge from the sample mixture.

In this technique, the sample is loaded onto an ion exchange column containing the charged resin or gel. As the sample moves through the column, ions in the sample compete for binding sites on the stationary phase with ions already present in the column. The ions that bind most strongly to the stationary phase will elute (come off) slower than those that bind more weakly.

Ion exchange chromatography can be performed using either cation exchangers, which exchange positive ions (cations), or anion exchangers, which exchange negative ions (anions). The pH and ionic strength of the mobile phase can be adjusted to control the binding and elution of specific ions.

Ion exchange chromatography is widely used in various applications such as water treatment, protein purification, and chemical analysis.

Diabetes Mellitus, Type 1 is a chronic autoimmune disease characterized by the destruction of insulin-producing beta cells in the pancreas, leading to an absolute deficiency of insulin. This results in an inability to regulate blood glucose levels, causing hyperglycemia (high blood sugar). Type 1 diabetes typically presents in childhood or early adulthood, although it can develop at any age. It is usually managed with regular insulin injections or the use of an insulin pump, along with monitoring of blood glucose levels and adjustments to diet and physical activity. Uncontrolled type 1 diabetes can lead to serious complications such as kidney damage, nerve damage, blindness, and cardiovascular disease.

Histidine is an essential amino acid, meaning it cannot be synthesized by the human body and must be obtained through dietary sources. Its chemical formula is C6H9N3O2. Histidine plays a crucial role in several physiological processes, including:

1. Protein synthesis: As an essential amino acid, histidine is required for the production of proteins, which are vital components of various tissues and organs in the body.

2. Hemoglobin synthesis: Histidine is a key component of hemoglobin, the protein in red blood cells responsible for carrying oxygen throughout the body. The imidazole side chain of histidine acts as a proton acceptor/donor, facilitating the release and uptake of oxygen by hemoglobin.

3. Acid-base balance: Histidine is involved in maintaining acid-base homeostasis through its role in the biosynthesis of histamine, which is a critical mediator of inflammatory responses and allergies. The decarboxylation of histidine results in the formation of histamine, which can increase vascular permeability and modulate immune responses.

4. Metal ion binding: Histidine has a high affinity for metal ions such as zinc, copper, and iron. This property allows histidine to participate in various enzymatic reactions and maintain the structural integrity of proteins.

5. Antioxidant defense: Histidine-containing dipeptides, like carnosine and anserine, have been shown to exhibit antioxidant properties by scavenging reactive oxygen species (ROS) and chelating metal ions. These compounds may contribute to the protection of proteins and DNA from oxidative damage.

Dietary sources of histidine include meat, poultry, fish, dairy products, and wheat germ. Histidine deficiency is rare but can lead to growth retardation, anemia, and impaired immune function.

Leghemoglobin is a type of protein known as a hemeprotein, found in the root nodules of leguminous plants (plants belonging to the family Fabaceae or Leguminosae). These root nodules are formed through a symbiotic relationship with nitrogen-fixing bacteria called Rhizobia.

The primary function of leghemoglobin is to facilitate the process of nitrogen fixation by maintaining an optimal oxygen concentration within the root nodule cells, where the Rhizobia reside. By binding and releasing oxygen reversibly, leghemoglobin protects the nitrogen-fixing enzyme, nitrogenase, from being inactivated by excess oxygen. This ensures that the Rhizobia can effectively convert atmospheric nitrogen gas (N2) into ammonia (NH3), which is then utilized by the plant for its growth and development.

In summary, leghemoglobin is a crucial protein in the process of biological nitrogen fixation, allowing leguminous plants to grow without the need for added nitrogen fertilizers.

Medical Definition:

"Risk factors" are any attribute, characteristic or exposure of an individual that increases the likelihood of developing a disease or injury. They can be divided into modifiable and non-modifiable risk factors. Modifiable risk factors are those that can be changed through lifestyle choices or medical treatment, while non-modifiable risk factors are inherent traits such as age, gender, or genetic predisposition. Examples of modifiable risk factors include smoking, alcohol consumption, physical inactivity, and unhealthy diet, while non-modifiable risk factors include age, sex, and family history. It is important to note that having a risk factor does not guarantee that a person will develop the disease, but rather indicates an increased susceptibility.

Hypoglycemic agents are a class of medications that are used to lower blood glucose levels in the treatment of diabetes mellitus. These medications work by increasing insulin sensitivity, stimulating insulin release from the pancreas, or inhibiting glucose production in the liver. Examples of hypoglycemic agents include sulfonylureas, meglitinides, biguanides, thiazolidinediones, DPP-4 inhibitors, SGLT2 inhibitors, and GLP-1 receptor agonists. It's important to note that the term "hypoglycemic" refers to a condition of abnormally low blood glucose levels, but in this context, the term is used to describe agents that are used to treat high blood glucose levels (hyperglycemia) associated with diabetes.

Altitude is the height above a given level, especially mean sea level. In medical terms, altitude often refers to high altitude, which is generally considered to be 1500 meters (about 5000 feet) or more above sea level. At high altitudes, the air pressure is lower and there is less oxygen available, which can lead to altitude sickness in some people. Symptoms of altitude sickness can include headache, dizziness, shortness of breath, and fatigue. It's important for people who are traveling to high altitudes to allow themselves time to adjust to the lower oxygen levels and to watch for signs of altitude sickness.

Erythroblastic Leukemia, Acute (also known as Acute Erythroid Leukemia or AEL) is a subtype of acute myeloid leukemia (AML), which is a type of cancer affecting the blood and bone marrow. In this condition, there is an overproduction of erythroblasts (immature red blood cells) in the bone marrow, leading to their accumulation and interference with normal blood cell production. This results in a decrease in the number of functional red blood cells, white blood cells, and platelets in the body. Symptoms may include fatigue, weakness, frequent infections, and easy bruising or bleeding. AEL is typically treated with chemotherapy and sometimes requires stem cell transplantation.

Transferrin is a glycoprotein that plays a crucial role in the transport and homeostasis of iron in the body. It's produced mainly in the liver and has the ability to bind two ferric (Fe3+) ions in its N-lobe and C-lobe, thus creating transferrin saturation.

This protein is essential for delivering iron to cells while preventing the harmful effects of free iron, which can catalyze the formation of reactive oxygen species through Fenton reactions. Transferrin interacts with specific transferrin receptors on the surface of cells, particularly in erythroid precursors and brain endothelial cells, to facilitate iron uptake via receptor-mediated endocytosis.

In addition to its role in iron transport, transferrin also has antimicrobial properties due to its ability to sequester free iron, making it less available for bacterial growth and survival. Transferrin levels can be used as a clinical marker of iron status, with decreased levels indicating iron deficiency anemia and increased levels potentially signaling inflammation or liver disease.

Hemolytic anemia, congenital is a type of anemia that is present at birth and characterized by the abnormal breakdown (hemolysis) of red blood cells. This can occur due to various genetic defects that affect the structure or function of the red blood cells, making them more susceptible to damage and destruction.

There are several types of congenital hemolytic anemias, including:

1. Congenital spherocytosis: A condition caused by mutations in genes that affect the shape and stability of red blood cells, leading to the formation of abnormally shaped and fragile cells that are prone to hemolysis.
2. G6PD deficiency: A genetic disorder that affects the enzyme glucose-6-phosphate dehydrogenase (G6PD), which is essential for protecting red blood cells from damage. People with this condition have low levels of G6PD, making their red blood cells more susceptible to hemolysis when exposed to certain triggers such as infections or certain medications.
3. Hereditary elliptocytosis: A condition caused by mutations in genes that affect the structure and flexibility of red blood cells, leading to the formation of abnormally shaped and fragile cells that are prone to hemolysis.
4. Pyruvate kinase deficiency: A rare genetic disorder that affects an enzyme called pyruvate kinase, which is essential for the production of energy in red blood cells. People with this condition have low levels of pyruvate kinase, leading to the formation of fragile and abnormally shaped red blood cells that are prone to hemolysis.

Symptoms of congenital hemolytic anemia can vary depending on the severity of the condition but may include fatigue, weakness, pale skin, jaundice, dark urine, and an enlarged spleen. Treatment may involve blood transfusions, medications to manage symptoms, and in some cases, surgery to remove the spleen.

Serum albumin is the most abundant protein in human blood plasma, synthesized by the liver. It plays a crucial role in maintaining the oncotic pressure or colloid osmotic pressure of blood, which helps to regulate the fluid balance between the intravascular and extravascular spaces.

Serum albumin has a molecular weight of around 66 kDa and is composed of a single polypeptide chain. It contains several binding sites for various endogenous and exogenous substances, such as bilirubin, fatty acids, hormones, and drugs, facilitating their transport throughout the body. Additionally, albumin possesses antioxidant properties, protecting against oxidative damage.

Albumin levels in the blood are often used as a clinical indicator of liver function, nutritional status, and overall health. Low serum albumin levels may suggest liver disease, malnutrition, inflammation, or kidney dysfunction.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

Retrospective studies, also known as retrospective research or looking back studies, are a type of observational study that examines data from the past to draw conclusions about possible causal relationships between risk factors and outcomes. In these studies, researchers analyze existing records, medical charts, or previously collected data to test a hypothesis or answer a specific research question.

Retrospective studies can be useful for generating hypotheses and identifying trends, but they have limitations compared to prospective studies, which follow participants forward in time from exposure to outcome. Retrospective studies are subject to biases such as recall bias, selection bias, and information bias, which can affect the validity of the results. Therefore, retrospective studies should be interpreted with caution and used primarily to generate hypotheses for further testing in prospective studies.

Osmotic fragility is a term used in medicine, specifically in the field of hematology. It refers to the susceptibility or tendency of red blood cells (RBCs) to undergo lysis (rupture or breaking open) when exposed to hypotonic solutions (solutions with lower osmotic pressure than the RBCs). This test is often used to diagnose and monitor hereditary spherocytosis, a genetic disorder that affects the structure and stability of red blood cells.

In this condition, the RBC membrane proteins are defective, leading to abnormally shaped and fragile cells. When these abnormal RBCs come into contact with hypotonic solutions, they rupture more easily than normal RBCs due to their decreased osmotic resistance. The degree of osmotic fragility can be measured through a laboratory test called the "osmotic fragility test," which evaluates the stability and structural integrity of RBCs in response to varying osmotic pressures.

In summary, osmotic fragility is a medical term that describes the increased susceptibility of red blood cells to lysis when exposed to hypotonic solutions, often associated with hereditary spherocytosis or other conditions affecting RBC membrane stability.

Pregnancy is a physiological state or condition where a fertilized egg (zygote) successfully implants and grows in the uterus of a woman, leading to the development of an embryo and finally a fetus. This process typically spans approximately 40 weeks, divided into three trimesters, and culminates in childbirth. Throughout this period, numerous hormonal and physical changes occur to support the growing offspring, including uterine enlargement, breast development, and various maternal adaptations to ensure the fetus's optimal growth and well-being.

Bloodletting is a medical procedure that was commonly used in the past to balance the four humors of the body, which were believed to be blood, phlegm, black bile, and yellow bile. The procedure involved withdrawing blood from a patient through various methods such as venesection (making an incision in a vein), leeches, or cupping.

The theory behind bloodletting was that if one humor became overabundant, it could cause disease or illness. By removing some of the excess humor, practitioners believed they could restore balance and promote healing. Bloodletting was used to treat a wide variety of conditions, including fever, inflammation, and pain.

While bloodletting is no longer practiced in modern medicine, it was once a common treatment for many different ailments. The practice dates back to ancient times and was used by various cultures throughout history, including the Greeks, Romans, Egyptians, and Chinese. However, its effectiveness as a medical treatment has been called into question, and it is now considered an outdated and potentially harmful procedure.

Reference values, also known as reference ranges or reference intervals, are the set of values that are considered normal or typical for a particular population or group of people. These values are often used in laboratory tests to help interpret test results and determine whether a patient's value falls within the expected range.

The process of establishing reference values typically involves measuring a particular biomarker or parameter in a large, healthy population and then calculating the mean and standard deviation of the measurements. Based on these statistics, a range is established that includes a certain percentage of the population (often 95%) and excludes extreme outliers.

It's important to note that reference values can vary depending on factors such as age, sex, race, and other demographic characteristics. Therefore, it's essential to use reference values that are specific to the relevant population when interpreting laboratory test results. Additionally, reference values may change over time due to advances in measurement technology or changes in the population being studied.

Erythroblasts are immature red blood cells that are produced in the bone marrow. They are also known as normoblasts and are a stage in the development of red blood cells, or erythrocytes. Erythroblasts are larger than mature red blood cells and have a nucleus, which is lost during the maturation process. These cells are responsible for producing hemoglobin, the protein that carries oxygen in the blood. Abnormal increases or decreases in the number of erythroblasts can be indicative of certain medical conditions, such as anemia or leukemia.

Nutritional status is a concept that refers to the condition of an individual in relation to their nutrient intake, absorption, metabolism, and excretion. It encompasses various aspects such as body weight, muscle mass, fat distribution, presence of any deficiencies or excesses of specific nutrients, and overall health status.

A comprehensive assessment of nutritional status typically includes a review of dietary intake, anthropometric measurements (such as height, weight, waist circumference, blood pressure), laboratory tests (such as serum albumin, total protein, cholesterol levels, vitamin and mineral levels), and clinical evaluation for signs of malnutrition or overnutrition.

Malnutrition can result from inadequate intake or absorption of nutrients, increased nutrient requirements due to illness or injury, or excessive loss of nutrients due to medical conditions. On the other hand, overnutrition can lead to obesity and related health problems such as diabetes, cardiovascular disease, and certain types of cancer.

Therefore, maintaining a good nutritional status is essential for overall health and well-being, and it is an important consideration in the prevention, diagnosis, and treatment of various medical conditions.

Erythroid precursor cells, also known as erythroblasts or normoblasts, are early stage cells in the process of producing mature red blood cells (erythrocytes) in the bone marrow. These cells are derived from hematopoietic stem cells and undergo a series of maturation stages, including proerythroblast, basophilic erythroblast, polychromatophilic erythroblast, and orthochromatic erythroblast, before becoming reticulocytes and then mature red blood cells. During this maturation process, the cells lose their nuclei and become enucleated, taking on the biconcave shape and flexible membrane that allows them to move through small blood vessels and deliver oxygen to tissues throughout the body.

Oxygen consumption, also known as oxygen uptake, is the amount of oxygen that is consumed or utilized by the body during a specific period of time, usually measured in liters per minute (L/min). It is a common measurement used in exercise physiology and critical care medicine to assess an individual's aerobic metabolism and overall health status.

In clinical settings, oxygen consumption is often measured during cardiopulmonary exercise testing (CPET) to evaluate cardiovascular function, pulmonary function, and exercise capacity in patients with various medical conditions such as heart failure, chronic obstructive pulmonary disease (COPD), and other respiratory or cardiac disorders.

During exercise, oxygen is consumed by the muscles to generate energy through a process called oxidative phosphorylation. The amount of oxygen consumed during exercise can provide important information about an individual's fitness level, exercise capacity, and overall health status. Additionally, measuring oxygen consumption can help healthcare providers assess the effectiveness of treatments and rehabilitation programs in patients with various medical conditions.

Chromium isotopes are different forms of the chemical element Chromium (Cr), which have different numbers of neutrons in their atomic nuclei. This results in each isotope having a different atomic mass, although they all have the same number of protons (24) and therefore share the same chemical properties.

The most common and stable chromium isotopes are Chromium-52 (Cr-52), Chromium-53 (Cr-53), Chromium-54 (Cr-54), and Chromium-56 (Cr-56). The other less abundant isotopes of Chromium, such as Chromium-50 (Cr-50) and Chromium-51 (Cr-51), are radioactive and undergo decay to become stable isotopes.

Chromium is an essential trace element for human health, playing a role in the metabolism of carbohydrates, lipids, and proteins. It is also used in various industrial applications, such as in the production of stainless steel and other alloys.

Methemoglobinemia is a medical condition characterized by an increased level of methemoglobin in the blood. Methemoglobin is a form of hemoglobin that cannot effectively transport oxygen throughout the body due to the iron atom within its structure being oxidized from the ferrous (Fe2+) state to the ferric (Fe3+) state.

Under normal circumstances, methemoglobin levels are kept below 1% of total hemoglobin. However, when these levels rise above 10%, it can lead to symptoms such as shortness of breath, headache, fatigue, and cyanosis (a bluish discoloration of the skin and mucous membranes). Severe methemoglobinemia, with levels exceeding 50%, can result in life-threatening complications, including seizures, coma, and even death.

Methemoglobinemia can be congenital or acquired. Congenital methemoglobinemia is caused by genetic defects affecting the enzymes responsible for reducing methemoglobin back to its functional form, hemoglobin. Acquired methemoglobinemia can result from exposure to certain medications, chemicals, or toxins that oxidize hemoglobin and increase methemoglobin levels. Treatment typically involves administering methylene blue, a reducing agent that helps convert methemoglobin back to functional hemoglobin. In severe cases or when methylene blue is contraindicated, alternative treatments such as exchange transfusions or hyperbaric oxygen therapy may be considered.

Amino acids are organic compounds that serve as the building blocks of proteins. They consist of a central carbon atom, also known as the alpha carbon, which is bonded to an amino group (-NH2), a carboxyl group (-COOH), a hydrogen atom (H), and a variable side chain (R group). The R group can be composed of various combinations of atoms such as hydrogen, oxygen, sulfur, nitrogen, and carbon, which determine the unique properties of each amino acid.

There are 20 standard amino acids that are encoded by the genetic code and incorporated into proteins during translation. These include:

1. Alanine (Ala)
2. Arginine (Arg)
3. Asparagine (Asn)
4. Aspartic acid (Asp)
5. Cysteine (Cys)
6. Glutamine (Gln)
7. Glutamic acid (Glu)
8. Glycine (Gly)
9. Histidine (His)
10. Isoleucine (Ile)
11. Leucine (Leu)
12. Lysine (Lys)
13. Methionine (Met)
14. Phenylalanine (Phe)
15. Proline (Pro)
16. Serine (Ser)
17. Threonine (Thr)
18. Tryptophan (Trp)
19. Tyrosine (Tyr)
20. Valine (Val)

Additionally, there are several non-standard or modified amino acids that can be incorporated into proteins through post-translational modifications, such as hydroxylation, methylation, and phosphorylation. These modifications expand the functional diversity of proteins and play crucial roles in various cellular processes.

Amino acids are essential for numerous biological functions, including protein synthesis, enzyme catalysis, neurotransmitter production, energy metabolism, and immune response regulation. Some amino acids can be synthesized by the human body (non-essential), while others must be obtained through dietary sources (essential).

Dicrocoelium is a genus of digenean flatworms, also known as liver flukes. These parasites primarily infect the livers of herbivorous animals, such as sheep and cattle, but can also occasionally infect humans. The medical definition of Dicrocoelium refers to these parasitic worms that have a complex life cycle involving snails, ants, and definitive hosts (herbivores or humans).

The most common species is Dicrocoelium dendriticum, which causes dicrocoeliasis in its definitive host. Infection occurs when the herbivore ingests vegetation contaminated with metacercariae, the infective stage of the parasite, encysted on the surface of plants. Once inside the definitive host, the metacercariae excyst and migrate to the bile ducts in the liver, where they mature into adults and produce eggs that are excreted in the feces.

The life cycle continues when these eggs are consumed by a specific type of snail, which becomes infected after ingesting the eggs. Inside the snail, the parasites undergo asexual reproduction, producing cercariae, which then leave the snail and encyst on the surface of vegetation or in ants. When an ant accidentally ingests these encysted cercariae, they migrate to the brain of the ant and manipulate its behavior, causing it to climb up tall blades of grass or other vegetation during the daytime. This exposes the ant to being eaten by a grazing herbivore, which completes the life cycle when it ingests the infected ant.

In humans, Dicrocoelium infection is rare and usually occurs after consuming raw or undercooked vegetables contaminated with metacercariae. Symptoms of dicrocoeliasis can include abdominal pain, diarrhea, weight loss, and liver enlargement. Diagnosis is typically made by detecting eggs in the stool, and treatment involves administering anthelmintic medications to eliminate the parasites from the body.

Blood proteins, also known as serum proteins, are a group of complex molecules present in the blood that are essential for various physiological functions. These proteins include albumin, globulins (alpha, beta, and gamma), and fibrinogen. They play crucial roles in maintaining oncotic pressure, transporting hormones, enzymes, vitamins, and minerals, providing immune defense, and contributing to blood clotting.

Albumin is the most abundant protein in the blood, accounting for about 60% of the total protein mass. It functions as a transporter of various substances, such as hormones, fatty acids, and drugs, and helps maintain oncotic pressure, which is essential for fluid balance between the blood vessels and surrounding tissues.

Globulins are divided into three main categories: alpha, beta, and gamma globulins. Alpha and beta globulins consist of transport proteins like lipoproteins, hormone-binding proteins, and enzymes. Gamma globulins, also known as immunoglobulins or antibodies, are essential for the immune system's defense against pathogens.

Fibrinogen is a protein involved in blood clotting. When an injury occurs, fibrinogen is converted into fibrin, which forms a mesh to trap platelets and form a clot, preventing excessive bleeding.

Abnormal levels of these proteins can indicate various medical conditions, such as liver or kidney disease, malnutrition, infections, inflammation, or autoimmune disorders. Blood protein levels are typically measured through laboratory tests like serum protein electrophoresis (SPE) and immunoelectrophoresis (IEP).

In the context of medical and biological sciences, a "binding site" refers to a specific location on a protein, molecule, or cell where another molecule can attach or bind. This binding interaction can lead to various functional changes in the original protein or molecule. The other molecule that binds to the binding site is often referred to as a ligand, which can be a small molecule, ion, or even another protein.

The binding between a ligand and its target binding site can be specific and selective, meaning that only certain ligands can bind to particular binding sites with high affinity. This specificity plays a crucial role in various biological processes, such as signal transduction, enzyme catalysis, or drug action.

In the case of drug development, understanding the location and properties of binding sites on target proteins is essential for designing drugs that can selectively bind to these sites and modulate protein function. This knowledge can help create more effective and safer therapeutic options for various diseases.

Erythrocyte deformability refers to the ability of red blood cells (erythrocytes) to change shape and bend without rupturing, which is crucial for their efficient movement through narrow blood vessels. This deformability is influenced by several factors including the cell membrane structure, hemoglobin concentration, and intracellular viscosity. A decrease in erythrocyte deformability can negatively impact blood flow and oxygen delivery to tissues, potentially contributing to various pathological conditions such as sickle cell disease, diabetes, and cardiovascular diseases.

Excessive glucose in the blood can attach to hemoglobin and raise the level of hemoglobin A1c. Hemoglobin and hemoglobin-like ... There is more than one hemoglobin gene. In humans, hemoglobin A (the main form of hemoglobin in adults) is coded by genes HBA1 ... Abnormal forms that occur in diseases: Hemoglobin D-Punjab - (α2βD2) - A variant form of hemoglobin. Hemoglobin H (β4) - A ... Hemoglobin A is the most intensively studied of the hemoglobin molecules. In human infants, the hemoglobin molecule is made up ...
Hemoglobin Gower 1 (also referred to as ζ2ε2 or HbE Gower-1) is a form of hemoglobin existing only during embryonic life, and ... Hemoglobin Gower 2 (also referred to as α2ε2 or HbE Gower-2) is a form of hemoglobin existing at low levels during embryonic ... Hemoglobin Portland I (also referred to as ζ2γ2 or HbE Portland-1) is a form of hemoglobin existing at low levels during ... Hemoglobin Portland II (also referred to as ζ2β2 or HbE Portland-2) is a form of hemoglobin existing at low levels during ...
The hemoglobin is now known as hemoglobin O-Arab. In 1974, another abnormal hemoglobin which they called hemoglobin O-Padova ... Hemoglobin O (HbO) is a rare type of hemoglobin in which there is a substitution of glutamic acid by lysine as in hemoglobin C ... The hemoglobin was eventually named hemoglobin O Indonesia. In 1960, a different but related hemoglobin was found from an 8- ... Hemoglobin O-Padova is the most severe form and is associated with disease of the RBCs and spleen. Hemoglobin O Indonesia is ...
... (HbA1c, glycohemoglobin, hemoglobin, A1C or A1c) is a form of hemoglobin (Hb) that is chemically linked to ... the more glucose binds to hemoglobin in the red blood cells and the higher the glycated hemoglobin. Once a hemoglobin molecule ... Hemoglobin A1c was first separated from other forms of hemoglobin by Huisman and Meyering in 1958 using a chromatographic ... Glycated hemoglobin is preferred over glycosylated hemoglobin to reflect the correct (non-enzymatic) process. Early literature ...
... is a blood test that can detect different types of hemoglobin. The test can detect hemoglobin S, the ... hemoglobin A2, which accounts for less than 3.5%; and a minute amount of hemoglobin F.: 140 If abnormal hemoglobin variants ... Hemoglobin A2 levels are typically elevated in beta-thalassemia minor and hemoglobin F may be slightly increased. In beta- ... 461-2 In hemoglobin H disease, a form of alpha-thalassemia, an abnormal band of hemoglobin H can be detected, and sometimes a ...
Some normal hemoglobin types are; Hemoglobin A (Hb A), which is 95-98% of hemoglobin found in adults, Hemoglobin A2 (Hb A2), ... Hemoglobin F is the primary hemoglobin produced by the fetus. The hemoglobin transports oxygen efficiently in a low oxygen ... Hb Lepore Hb M Hb F Hb Hope Hb Pisa Hb J Hb Barts Hb N-Baltimore Hemoglobin Chesapeake Hemoglobin Louisville Hemoglobin ... Hemoglobin variants are different types of hemoglobin molecules, by different combinations of its subunits and/or mutations ...
Vitreoscilla haemoglobin (VHb) is a type of haemoglobin found in the Gram-negative aerobic bacterium, Vitreoscilla. It is the ... first haemoglobin discovered from bacteria, but unlike classic hemoglobin it is composed only of a single globin molecule. VHb ... Stark BC, Dikshit KL, Pagilla KR (2012). "The Biochemistry of Vitreoscilla hemoglobin". Computational and Structural ... Articles with short description, Short description is different from Wikidata, Hemoglobins). ...
... the composition of hemoglobin is hemoglobin A (~97%), hemoglobin A2 (2.2 - 3.5%) and hemoglobin F (. 70% of total hemoglobin ... Hemoglobin F, like adult hemoglobin (hemoglobin A and hemoglobin A2), has four subunits or chains. Each subunit contains a heme ... Fetal hemoglobin, or foetal haemoglobin (also hemoglobin F, HbF, or α2γ2) is the main oxygen carrier protein in the human fetus ... At birth, hemoglobin F accounts for 50-95% of the infant's hemoglobin and at around 6 months after birth, hemoglobin A becomes ...
... is a predominantly historic term for a fraction of normal hemoglobin molecules that is seen when hemoglobin is ... As these Hemoglobin subtypes are formed over time, they are found more prevalent in older red cells. Hemoglobin Maxwell Myer, ... These Hemoglobin molecules are non-enzymatic modifications of the hemoglobin molecules and they encompass hemoglobinA1c, Hb1a ( ... Hemoglobins, All stub articles, Cell biology stubs). ...
... fetal hemoglobin). In the first months of life, fetal hemoglobin disappears and the amount of hemoglobin E increases, so the ... Hemoglobin E (HbE) is an abnormal hemoglobin with a single point mutation in the β chain. At position 26 there is a change in ... People who have hemoglobin E/β-thalassemia have inherited one gene for hemoglobin E from one parent and one gene for β- ... This is called hemoglobin E trait, and it is not a disease. People who have hemoglobin E trait (heterozygous) are asymptomatic ...
... (HbA2) is a normal variant of hemoglobin A that consists of two alpha and two delta chains (α2δ2) and is found at ... Hemoglobin+A2 at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Hemoglobin A2 - The clinical ... Hemoglobin A2 may be increased in beta thalassemia or in people who are heterozygous for the beta thalassemia gene. HbA2 exists ... in small amounts in all adult humans (1.5-3.1% of all hemoglobin molecules) and is approximately normal in people with sickle- ...
Hemoglobin Hemoglobin variants: Hb A1C Hemoglobin A2 Hemoglobin C Hemoglobin F Hemoglobin O Hemoglobin protein subunits (genes ... This hemoglobin makes up 1-3% of hemoglobin in adults. Hemoglobin A (HbA) is the most common adult form of hemoglobin and ... Hemoglobin A (HbA), also known as adult hemoglobin, hemoglobin A1 or α2β2, is the most common human hemoglobin tetramer, ... Hemoglobin A is the most common adult form of hemoglobin and exists as a tetramer containing two alpha subunits and two beta ...
Hemoglobin G, Hemoglobin G-Philadelphia, or hbG, is a mutation of the cells that oxygenate blood. The G-Philadelphia variant is ... "Combinations of Hemoglobin G, Hemoglobin S and Thalassemia Occurring in One Family". Blood. 12 (3): 238-250. CiteSeerX 10.1. ... "Anemia Associated with Hemoglobin G-Philadelphia". 2019-01-17. Schwartz, H. C.; Spaet, T. H.; Zuelzer, W. W.; Neel, J. V.; ... Schwartz et al confirmed that Hemoglobin G is a normal mutation of the combination of S and A alleles, which is reflected in ...
... (F-Hb) usually refers to hemoglobin in blood from rectal bleeding (fecal hemoglobin), but may also refer to ... Hemoglobin F (fetal hemoglobin). This disambiguation page lists articles associated with the title F-Hemoglobin. If an internal ...
... is a predicted protein encoded in the HBM gene. The mRNA is expressed at moderate levels, but the protein has not ...
... , abbreviated Hb Barts, is an abnormal type of hemoglobin that consists of four gamma globins. It is moderately ... The ability to measure hemoglobin Barts makes it useful in newborn screening tests. If hemoglobin Barts is detected on a ... This variant of hemoglobin is so called as it was discovered at St Bartholomew's Hospital in London, often abbreviated to Barts ... Since hemoglobin Barts is elevated in alpha thalassemia, it can be measured, providing a useful screening test for this disease ...
... reported from Meerut India shows the mutation of 120th alanine to glutamic acid on alpha chain. Hemoglobin J was ... Hemoglobin J is an abnormal hemoglobin, an alpha globin gene variant and present in various geographic locations. It was first ... Blackwell, R (May 10, 1974). "Hemoglobin J Meerut: alpha120 Ala leads to Glu". Biochim Biophys Acta. 351 (1): 7-12. doi:10.1016 ... "Hemoglobin j". Science. 123 (3203): 889-890. Bibcode:1956Sci...123..889T. doi:10.1126/science.123.3203.889. PMID 13324107. ...
The hemoglobin was named hemoglobin III, but hemoglobin C was eventually used. By 1954, it was found that the mutant hemoglobin ... Their red blood cells contain both hemoglobin C and either normal hemoglobin A or hemoglobin S. Hemoglobin C mutation is an ... and the gene for hemoglobin C; this state is called hemoglobin SC disease, and is generally more severe than hemoglobin C ... of African-Americans have hemoglobin S (Sickle) gene. Thus Hemoglobin SC disease is significantly more common than Hemoglobin ...
... (beta globin, β-globin, haemoglobin beta, hemoglobin beta) is a globin protein, coded for by the HBB ... HBB interacts with Haemoglobin, alpha 1 (HBA1) to form haemoglobin A, the major haemoglobin in adult humans. The interaction is ... Sickle cell disease is closely related to another mutant haemoglobin called haemoglobin C (HbC), because they can be inherited ... Hemoglobin subunit alpha Human β-globin locus GRCh38: Ensembl release 89: ENSG00000244734 - Ensembl, May 2017 GRCm38: Ensembl ...
... is a protein that in humans is encoded by the HBZ gene. Zeta-globin is an alpha-like hemoglobin. The ... "Entrez Gene: HBZ hemoglobin, zeta". Giardina B, Messana I, Scatena R, Castagnola M (1995). "The multiple functions of ... Luo HY, Liang XL, Frye C, Wonio M, Hankins GD, Chui DH, Alter BP (July 1999). "Embryonic hemoglobins are expressed in ... Clegg JB, Gagnon J (October 1981). "Structure of the zeta chain of human embryonic hemoglobin". Proceedings of the National ...
Hemoglobin S is the most common abnormal hemoglobin variant. Hemoglobin S is the variant that causes sickle cell, which is a ... Hemoglobin S has two beta chains, whereas hemoglobin Hopkins-2 has two alpha chains. Hopkins-2 makes up 22% of hemolysates in ... Hemoglobin Hopkins-2 (Hb Hop-2) is a mutation of the protein hemoglobin, which is responsible for the transportation of oxygen ... The deoxygenation of hemoglobin in sickle cell patients has severe implications on those who carry the mutation. The hemoglobin ...
... is a variant of hemoglobin in which a mutation in the alpha globin gene produces an alpha globin ... Hemoglobin Constant Spring is renamed after Constant Spring district in Jamaica. Hemoglobin variants Hemoglobinopathy ... It is the most common nondeletional alpha-thalassemia mutation associated with hemoglobin H disease. The quantity of hemoglobin ... Thalassemia What is Thalassemia? Hemoglobin H Disease and its Variants Hemoglobinopathiesm(Hemoglobin Disorders) Schrier, SL; ...
People with hemoglobin D trait have slightly more hemoglobin A than hemoglobin D. The abnormal hemoglobin is called hemoglobin ... Studies indicate that Hemoglobin D-Punjab accounts for over 55% of the total hemoglobin variants there. Hemoglobin D is a ... Normal red blood cells have hemoglobin A. People with hemoglobin D trait have red blood cells that have normal hemoglobin A ( ... Hemoglobin D-Punjab is one of the sub-variants of Hemoglobin D, a variant of hemoglobin found in human blood. It is so named ...
Vichinsky, E. P.; Lubin, B. H. (May 1980). "Unstable hemoglobins, hemoglobins with altered oxygen affinity, and m-hemoglobins ... Hemoglobin M disease is often not life-threatening and there is no known effective treatment. Hemoglobin M disease is a ... Hemoglobin M disease is a rare form of hemoglobinopathy, characterized by the presence of hemoglobin M (HbM) and elevated ... Cyanosis is the most common sign of hemoglobin M disease, which can be observed in all kinds of hemoglobin M diseases. It is ...
The amount of Hb Lepore in the patients blood ranged from 8 to 30%, the remainder being fetal hemoglobin (Hb F) which is ... Hemoglobin Lepore syndrome is typically an asymptomatic hemoglobinopathy, which is caused by an autosomal recessive genetic ... a blood disorder that reduces the production of the iron-containing protein hemoglobin which carries oxygen to cells and which ...
... (American English) or Haemoglobin O-Arab (British English) is a rare alternation of Hemoglobin (American ... When combined with Hemoglobin S (β^6Glu → Val) it causes a severe form of Sickle cell disease known as Hemoglobin S/O-Arab. ... When Hemoglobin O-Arab co-inherits with Hemoglobin S, it produces a syndrome with similarities in severity to sickle cell ... Hemoglobin C and hemoglobin O-Arab variants can be diagnosed using the Bio-Rad Variant II high-performance liquid ...
... , Hemoglobin, alpha 1, is a hemoglobin protein that in humans is encoded by the HBA1 gene. The human ... Hemoglobin subunit alpha has been shown to interact with hemoglobin subunit beta (HBB). Hemoglobin subunit beta Human β-globin ... 1992). "Six rare hemoglobin variants found in Sicily". Hemoglobin. 15 (5): 431-7. doi:10.3109/03630269108998862. PMID 1802885. ... which with fetal hemoglobin (HbF) makes up the remaining 3% of adult hemoglobin. Alpha thalassemias result from deletions of ...
The most common hemoglobin found within adult red blood cells is Hemoglobin A. The structure of Hb A consists of two α-globin ... Hemoglobin H (Hb H) Disease, also called alpha-thalassemia intermedia, is a disease affecting hemoglobin, the oxygen carrying ... Hemoglobin F is the predominant for in the fetus and it also contains α-globin, thus, in severe cases the disease can affect ... Hemoglobin H disease is a genetic disorder resulting in absent or impaired production of the α-globin protein, a normal ...
The mean corpuscular hemoglobin, or "mean cell hemoglobin" (MCH), is the average mass of hemoglobin (Hb) per red blood cell ( ... The amount of hemoglobin per RBC depends on hemoglobin synthesis and the size of the RBC.[citation needed] The mass of the red ... It is calculated by dividing the total mass of hemoglobin by the number of red blood cells in a volume of blood. MCH=(Hb*10)/ ... "Mean Cell Hemoglobin". Archived from the original on 2004-11-20. Retrieved 2009-03-03. Niemand, Hans Georg; Arnold-Gloor, Susi ...
... also known as HBA2 is a gene that in humans codes for the alpha globin chain of hemoglobin. The human alpha ... Deletion of all 4 alleles is lethal because it renders the body unable to make fetal hemoglobin (HbF), adult hemoglobin (HbA) ... fetal hemoglobin) makes up the remaining 3% of adult hemoglobin. Alpha-thalassemias most commonly result from deletions of any ... Zhu C, Yu W, Xie J, Chen L, Ding H, Shang X, Xu X (Oct 2010). "Hemoglobin H disease due to a de novo mutation at the α2-globin ...
Excessive glucose in the blood can attach to hemoglobin and raise the level of hemoglobin A1c. Hemoglobin and hemoglobin-like ... There is more than one hemoglobin gene. In humans, hemoglobin A (the main form of hemoglobin in adults) is coded by genes HBA1 ... Abnormal forms that occur in diseases: Hemoglobin D-Punjab - (α2βD2) - A variant form of hemoglobin. Hemoglobin H (β4) - A ... Hemoglobin A is the most intensively studied of the hemoglobin molecules. In human infants, the hemoglobin molecule is made up ...
The hemoglobin test measures how much hemoglobin is in your blood. ... Hemoglobin is a protein in red blood cells that carries oxygen. ... LOWER THAN NORMAL HEMOGLOBIN. Low hemoglobin level may be due ... Hemoglobin is a protein in red blood cells that carries oxygen. The hemoglobin test measures how much hemoglobin is in your ... HIGHER THAN NORMAL HEMOGLOBIN. High hemoglobin level is most often caused by low oxygen levels in the blood (hypoxia), present ...
Once formed, hemoglobin A1c is stable. As a result, the hemoglobin A1c level reflects the average blood glucose level over the ... Hemoglobin variants and hemoglobin A1c analysis: problem solved?. Clin Chem. 2003 Aug. 49(8):1245-7. [QxMD MEDLINE Link]. ... Hemoglobin A1c is a specific fraction of hemoglobin A found in healthy individuals as well as individuals with diabetes ... Hemoglobin A1c (glycated hemoglobin) reflects the average blood glucose concentration over the course of the red blood cell ( ...
Hemoglobin is a protein in red blood cells that transports oxygen around the body. Learn about symptoms, risks, and treatment ... How are hemoglobin levels tested?. A blood test can assess hemoglobin levels. This is called a hemoglobin test. Doctors may ... Each hemoglobin protein contains four iron atoms and can therefore carry four molecules of oxygen. Hemoglobin attaches to red ... Hemoglobin. (n.d.). https://medlineplus.gov/lab-tests/hemoglobin-test. *. Lee, G., et al. (2018). Association of hemoglobin ...
Measurements from healthy blood donors to study the physiologic variation of hemoglobin and platelet levels by changes in ... Blood Hemoglobin Concentration & Elevation (effect of atmospheric pressure on blood hemoglobin). Besides age, race, gender and ... Blood Hemoglobin By Race & Elevation. Variations in average hemoglobin concentrations among healthy donors were also observed ... Blood Hemoglobin & Elevation Correlation. Higher mean hemoglobin levels were observed among donors at higher altitudes for both ...
Hemoglobin has always been hemoglobin-theres no evidence it evolved. Did hemoglobin evolve? Evolutionists should be able to ... Hemoglobin has always been hemoglobin no matter where it is found. For example, many deep-ocean trenches have hydrothermal ... The red color is from several complex hemoglobins that have 144 globin chains. "The high molecular mass hemoglobin of the worm ... The structures are called embryonic (there are three types) and fetal hemoglobin (HbF), and they differ from adult hemoglobin ( ...
The high-resolution X-ray structures of the deoxy forms of four recombinant hemoglobins in which Trp37(C3)beta is replaced with ... High-resolution crystal structures of human hemoglobin with mutations at tryptophan 37beta: structural basis for a high- ... HEMOGLOBIN (VAL BETA1 MET) MUTANT. *PDB DOI: https://doi.org/10.2210/pdb1A0Z/pdb ...
Jean tested Chelles hemoglobin level. Hemoglobin is a substance in red blood cells that contains iron, and transports oxygen. ... Prenatal EFT improves hemoglobin count with before and after test Important Note: This article was written prior to 2010 and is ... Even though my hemoglobin was low before, that was fear-related ... that was my fear of hemorrhage, and Im free of that now. ... Even though my hemoglobin was low before, that was then. My body already has made changes, now that the fear has been released. ...
Youll also learn about some of the potential causes of high or low hemoglobin levels, and what hemoglobin A1c refers to. ... Well go over normal hemoglobin ranges for adults, children, and infants. ... Normal hemoglobin levels can vary based on several factors, including age and sex. ... sometimes called glycated hemoglobin. An HbA1c test measures the amount of glycated hemoglobin, which is hemoglobin that has ...
... Anne de Jong jonga at biol.rug.nl Fri Jan 31 07:58:59 EST 1997 *Previous message: x ... Why not measuring the leakage of hemoglobin from erythrocytes not at 430nm instead of 540 nm. *Previous message: x ...
Is routine hemoglobin and hematocrit testing on admission to labor and delivery needed?. Obstet Gynecol. December 2001;98:1038- ... If hemoglobin and hematocrit values are acceptable at that time, retesting later in pregnancy is not necessary in low-risk ... By the time the women were admitted in labor, the mean hemoglobin and hematocrit values had increased by a mean of 0.5 g per dL ... Hemoglobin and hematocrit measurements are performed in almost all women admitted to a hospital in labor. Sherard and Newton ...
Convergent evolution of hemoglobin. Denyse OLeary. October 4, 2016. Convergent evolution, News. Share. Facebook Twitter ...
hemoglobin. Why Hemoglobin A1c Is Not a Reliable Marker. Hemoglobin A1c is being increasingly used as a way to screen for ...
Evolution of Hemoglobin and Its Genes. Ross C. Hardison. Transcriptional Mechanisms Underlying Hemoglobin Synthesis. Koichi R. ... Hemoglobin and Its Diseases. Subject Area(s): Human Biology and Disease; Biochemistry. Edited by David Weatherall, Weatherall ... Hemoglobin and its Disorders: 150 Years of Study. David J. Weatherall, Alan N. Schechter, and David G. Nathan. Erythopoiesis: ... The Hemoglobin E Thalassemias. Suthat Fucharoen and David J. Weatherall. Clinical Manifestations of α-Thalassemia. Elliott P. ...
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... *Download PDF Copy ... Hemoglobin is the oxygen-carrying component of red blood cells, and with sickle cell disease its inefficient at this ... Fetal hemoglobin enables a developing baby to capture oxygen from mothers blood while the beta-globin gene produces adult ... That is important for sickle cell because we know in adults that the fetal hemoglobin gene is shut down and we know fetal ...
Hemoglobin and iron levels were measured seven times during the study. Compared to donors who did not take iron, the donors ... The study measured the effect of low dose daily iron supplementation on the time to recovery of lost hemoglobin and iron after ... The results of the Hemoglobin and Iron Recovery Study (HEIRS), supported by NIHs National Heart, Lung, and Blood Institute ( ... Study shows that iron supplementation after blood donation shortens hemoglobin recovery time ...
The gamma chain of fetal hemoglobin binds BPG with a lower affinity relative to the adult hemoglobin. This means that the fetal ... What role does BPG play in transfer of oxygen from the maternal hemoglobin (HbA) to the fetal hemoglobin (HbF)?. ... D-2-3 Bisphosphoglycerate decreases the affinity hemoglobin for oxygen by binding to and stabilizing the deoxy-hemoglobin state ... What mutation in hemoglobin causes sickle cell?. Definition. Mutation of glutamate (Glu) 6 to a valine (Val). Glu 6 is located ...
Get contact details and address of Hemoglobin Testing Services firms and companies in Hyderabad. ... Hemoglobin Testing Services Providers in Hyderabad, Telangana. ...
We did a secondary analysis of patients with chronic kidney disease enrolled in the Correction of Hemoglobin in the Outcomes in ... significantly more patients in the high-hemoglobin compared to the low-hemoglobin arm were unable to achieve target hemoglobin ... Secondary analysis of the CHOIR trial epoetin-alpha dose and achieved hemoglobin outcomes Kidney Int. 2008 Sep;74(6):791-8. doi ... We did a secondary analysis of patients with chronic kidney disease enrolled in the Correction of Hemoglobin in the Outcomes in ...
hemoglobin-alpha. [Alpha-hemoglobin; Alpha-globin] abbr. HbA. See: hemoglobin.. ... ... ... ... ... Subscribe to continue ... Hemoglobin A2. Next entry:. Hemoglobin-alpha-1. Random entry:. peptidylprolyl isomerase B. ...
Hemoglobin Electrophoresis, Thyroid Function, and Newborn Screening in Refugee Populations ... Hemoglobin E Trait. Hemoglobin E trait is frequently present in certain refugee groups, particularly among those from Southeast ... The prevalence of hemoglobin E trait is very high in parts of Southeast Asia - nearly 60% in regions of Thailand, Laos, and ... Source: Inherited Hemoglobin Disorders, edited by Anjana Munshi, ISBN 978-953-51-2198-5, Published: November 11, 2015. ...
Hemoglobin A1C More than 600 associates work 24/7 to process and report results. ...
Fetal hemoglobin (HbF) is the type of hemoglobin produced by a fetuss body. At birth, babies typically have half fetal ... hemoglobin and half adult hemoglobin (HbA). After birth, HbF is gradually replaced by HbA. With certain diseases, such as ... Hemoglobin is the oxygen-carrying substance in red blood cells. ...
Protein target information for Hemoglobin subunit beta (minke whale). Find diseases associated with this biological target and ...
Consequences of the COVID 19 Pandemic Reduced Hemoglobin A1c Consequences of the COVID-19 Pandemic: Reduced Hemoglobin A1c ... Consequences of the COVID-19 Pandemic: Reduced Hemoglobin A1c Diabetes Monitoring. Authors: Fragala MS, Kaufman HW, Meigs JB, ...
Robert T.S. Jim, Marina T. Yarbro; Survey of Haemoglobin Types in Hawaii. Acta Haematol 1 June 1960; 23 (6): 398-400. https:// ...
Core tip: It is unheard of in the medical history to take up a patient with hemoglobin of 2 g/dL for anesthesia and major bowel ... He had an extremely low hemoglobin level (2 g/dL) and mild renal and hepatic impairment. He was immediately admitted for right ... Keywords: Gastrointestinal bleed, Low hemoglobin level, Jehovahs witnesses, Multiple terminal ileal ulceration, Enterotomy, ... Successful bowel surgery at hemoglobin 2 g/dL without blood transfusion. World J Gastrointest Surg 2013; 5(8): 252-255 [PMID: ...
Home/Haemoglobin Disorders. Haemoglobin Disorders. Haemoglobin disorders or haemoglobinopathies are a group of conditions ... These are known as haemoglobin variants and they alter the function of the whole haemoglobin molecule. The most common of these ... Any disturbance of this structure of the haemoglobin molecule, reduces the capacity of the haemoglobin to carry oxygen to the ... The globin part of haemoglobin is a protein that consists of the alpha (α) and beta (β) parts or chains, which are produced by ...
Using an Advanced Practice Pharmacist in a Team-Based Care Model to Decrease Time to Hemoglobin A1c Goal Among Patients With ... Only half of the patients with diabetes achieve a glycated hemoglobin A1c (HbA1c) of less than 7% (1), despite the availability ... Abbreviations: BMI, body mass index; HbA1c, glycated hemoglobin A1c; PPM, pharmacist-physician managed; SD, standard deviation ... Cowart K, Sando K. Pharmacist impact on treatment intensification and hemoglobin A1C in patients with type 2 diabetes mellitus ...
  • Screening should include hemoglobin electrophoresis, particularly in individuals with anemia, red blood cell abnormalities, and/or morbidity suggestive of disease. (cdc.gov)
  • Hemoglobin electrophoresis measures the levels of the different types of this protein in t. (stlukes-stl.com)
  • This was a descriptive retrospective study of hemoglobin variants performed by electrophoresis in patients treated at and/or referred to specialized care institutions in Bogota, Colombia between January 2009 and December 2020. (scielo.br)
  • Sickling is identified in a sickling preparation, and hemoglobin electrophoresis establishes the diagnosis. (msdmanuals.com)
  • Methemoglobinemia can be acquired (exposure to oxidants) or inherited (i.e. decreased enzyme activity or presence of hemoglobin M). Acquired methemoglobinemia will have normal enzyme assay activity tests and normal Hb electrophoresis. (cdc.gov)
  • Hemoglobin electrophoresis is abnormal in HbM disease, but normal with NADH-methemoglobin reductase deficiency [McKenzie 2010]. (cdc.gov)
  • Representation of a human hemoglobin protein molecule. (icr.org)
  • Clinically relevant updates of the HbVar database of human hemoglobin variants and thalassemia mutations. (degruyter.com)
  • The βLys66Tyr Variant of Human Hemoglobin as a Component of a Blood Substitute. (lu.se)
  • It has been proposed that introducing tyrosine residues into human hemoglobin (e.g. βPhe41Tyr) may be able to reduce the toxicity of the ferryl heme species in extracellular hemoglobin-based oxygen carriers (HBOC) by facilitating long-range electron transfer from endogenous and exogenous antioxidants. (lu.se)
  • article{3b754337-9c40-4bb9-9b3f-7d78cf72497f, abstract = {{It has been proposed that introducing tyrosine residues into human hemoglobin (e.g. βPhe41Tyr) may be able to reduce the toxicity of the ferryl heme species in extracellular hemoglobin-based oxygen carriers (HBOC) by facilitating long-range electron transfer from endogenous and exogenous antioxidants. (lu.se)
  • Variations in the normal hemoglobin levels among healthy human donors based on their gender and blood collection centers is shown here. (redcross.org)
  • some patients even have normal hemoglobin levels. (msdmanuals.com)
  • The mammalian hemoglobin molecule can bind and transport up to four oxygen molecules. (wikipedia.org)
  • From the known atomic mass of iron, he calculated the molecular mass of hemoglobin to n × 16000 (n = number of iron atoms per hemoglobin molecule, now known to be 4), the first determination of a protein's molecular mass. (wikipedia.org)
  • Who would consider seriously a phylogeny of vertebrates drawn from a comparison of myoglobin [a single polypeptide chain molecule found in the muscles of vertebrates] of some species and hemoglobin from others? (icr.org)
  • The hemoglobin molecule is designed with much variation to supply the oxygen needs of a wide variety of organisms. (icr.org)
  • Haemoglobin disorders or haemoglobinopathies are a group of conditions affecting the molecule haemoglobin which is contained in the red blood cells. (thalassaemia.org.cy)
  • Any disturbance of this structure of the haemoglobin molecule, reduces the capacity of the haemoglobin to carry oxygen to the tissues , but also disturbs the whole structure of the red blood cell containing the haemoglobin. (thalassaemia.org.cy)
  • These are known as haemoglobin variants and they alter the function of the whole haemoglobin molecule. (thalassaemia.org.cy)
  • Overview of Hemoglobinopathies Hemoglobinopathies are genetic disorders affecting the structure or production of the hemoglobin molecule. (msdmanuals.com)
  • The name hemoglobin is derived from the words heme and globin, reflecting the fact that each subunit of hemoglobin is a globular protein with an embedded heme group. (wikipedia.org)
  • Hemoglobin consists of protein subunits (globin molecules), which are polypeptides, long folded chains of specific amino acids which determine the protein's chemical properties and function. (wikipedia.org)
  • The red color is from several complex hemoglobins that have 144 globin chains. (icr.org)
  • There are over 300 alleles (one of two or more forms of a gene that produce variations in a given trait) for the hemoglobin gene, part of the globin gene superfamily. (icr.org)
  • Contributors examine the structure, expression, and evolution of the globin genes, the assembly of globin subunits into functional forms of hemoglobin, and the numerous variants that result from genetic alterations. (cshlpress.com)
  • Histone deacetylases, or HDACs, are enzymes that are among the many ways gene expression gets turned down, a natural process for some genes, like the gamma-globin gene that makes fetal hemoglobin, as we move from childhood to adulthood. (news-medical.net)
  • Fetal hemoglobin enables a developing baby to capture oxygen from mother's blood while the beta-globin gene produces adult hemoglobin that carries oxygen. (news-medical.net)
  • The globin part of haemoglobin is a protein that consists of the alpha (α) and beta (β) parts or chains, which are produced by the α-globin genes and β-globin genes. (thalassaemia.org.cy)
  • Disorders can be divided into two main groups: qualitative alterations, in which there are variants in the globin genes that can cause changes in the structure of the globin and lead to the production of abnormal hemoglobin (HbS, HbC and HbE, among others) and quantitative alterations, which result from a quantitative deficiency in one or more of the hemoglobin globin chains (thalassemias). (scielo.br)
  • Automated detection of unstable hemoglobin variants by Sysmex XE-Series analyzers. (degruyter.com)
  • To evaluate the frequency of hemoglobin variants according to the geographical region in a population group adjusted to sex and age in Colombia. (scielo.br)
  • With new hemoglobin variants continuing to emerge, reviewing some of the rare hemoglobinopathies is prudent to support the anesthesia community in their assessment and care of patients who present with unexpectedly low SPO2 . (bvsalud.org)
  • Hemoglobin A1c (glycated hemoglobin) reflects the average blood glucose concentration over the course of the red blood cell (RBC) lifespan, roughly 120 days in normal individuals. (medscape.com)
  • Gain insights on measurements from healthy blood donors to study the physiologic variation of hemoglobin and platelet concentration levels by changes in altitude, geographic location, seasonal variations, age, race and sex. (redcross.org)
  • A non-linear relationship was observed between altitude and the mean hemoglobin concentration. (redcross.org)
  • Mild anemia corresponds to a level of hemoglobin concentration of 10.0-10.9 g/dl for pregnant women and children under age 5 and 10.0-11.9 g/dl for nonpregnant women. (meltingpointathens.com)
  • Procedures -Horses performed 1 preliminary exercise test (EXT) and 2 experimental EXT. Arterial and mixed venous blood samples and hemodynamic measurements were taken during the last 30 seconds of each step of the GXT to measure PO 2 , hemoglobin concentration ([Hb]), SO 2 , and determinants of acidbase state (protein, electrolytes, and PCO 2 ). (avma.org)
  • The extent of hemoglobin glycation is related not only to the glucose concentration in blood but also to the average RBC lifespan. (medscape.com)
  • Maternal hemoglobin concentration at delivery, umbilical cord hemoglobin and ferritin were collected. (bvsalud.org)
  • When having blood work done, you might also see results for hemoglobin A1c (HbA1c) , sometimes called glycated hemoglobin. (healthline.com)
  • An HbA1c test measures the amount of glycated hemoglobin, which is hemoglobin that has glucose attached to it, in your blood. (healthline.com)
  • The RIQAS Glycated Haemoglobin (HbA1c) EQA programme is designed to monitor the performance of HbA1c and Total Haemoglobin assays. (randox.com)
  • Annual hemoglobin A1c (HbA1c) tests are recommended for all diabetics, but some patient populations may face barriers to high quality healthcare that are beyond providers' control. (harvard.edu)
  • The gamma chain of fetal hemoglobin binds BPG with a lower affinity relative to the adult hemoglobin. (flashcardmachine.com)
  • This means that the fetal hemoglobn has a higher affinity for oxygen than the adult hemoglobin and transfer of oxygen from the low affinity HbA to the higher affinity HbF is thus enabled. (flashcardmachine.com)
  • Hemoglobin (also spelled haemoglobin, abbreviated Hb or Hgb), is the iron-containing oxygen-transport protein present in erythrocytes (red blood cells) of almost all vertebrates (the exception being the fish family Channichthyidae) as well as the tissues of some invertebrate animals. (wikipedia.org)
  • Hemoglobin in blood carries oxygen from the respiratory organs (lungs or gills) to the other tissues of the body, where it releases the oxygen to enable aerobic respiration which powers the animal's metabolism. (wikipedia.org)
  • In these tissues, hemoglobin absorbs unneeded oxygen as an antioxidant, and regulates iron metabolism. (wikipedia.org)
  • Hemoglobin is an iron-rich protein in red blood cells that enables the blood to carry oxygen to tissues throughout the body. (medicalnewstoday.com)
  • Then, as the blood flows through the tissues, hemoglobin releases its oxygen and changes shape to the deoxygenated form, causing release of the nitric oxide. (rcsb.org)
  • A light sensor containing two light sources (red and infra-red) transmits light through tissues, is absorbed by haemoglobin and detected by a photo sensor. (who.int)
  • The pathophysiological consequences of hemoglobin disorders (e.g., ineffective erythropoiesis and aberrant iron homeostasis), their clinical manifestations, and epidemiological trends are also described. (cshlpress.com)
  • This book includes discussions of management and treatment strategies for hemoglobin disorders, such as transfusions, iron-chelating agents, gene therapy, and stem cell transplantation. (cshlpress.com)
  • The drugs are called HDAC inhibitors, and the investigators have early evidence one called panobinostat can reactivate after birth the gene that produces fetal hemoglobin, which cannot sickle, says Abdullah Kutlar, MD, director of the Center for Blood Disorders at the Medical College of Georgia and Augusta University Health. (news-medical.net)
  • H emoglobin diseases are a group of blood disorders passed down through families in which there is an abnormal production or structure of the hemoglobin protein. (ms.gov)
  • If a test reveals that the hemoglobin level in an individual's body is lower than normal, it means that they have a low RBC count and are prone to disorders such as anemia. (imarcgroup.com)
  • Most disorders affecting hemoglobin are hereditary and it is estimated that approximately 7% of the world's population is constituted by carriers of different inherited hemoglobin disorders, making them the most common recessive hereditary diseases. (scielo.br)
  • Within hemoglobinopathies, sickle cell disease is the most common and is mainly widespread in sub-Saharan Africa, the Middle East, India and among people of African descent living in Europe and North, Central and South America 4 4 Cataldo F. Immigration and changes in the epidemiology of hemoglobin disorders in Italy: an emerging public health burden. (scielo.br)
  • 4 4 Cataldo F. Immigration and changes in the epidemiology of hemoglobin disorders in Italy: an emerging public health burden. (scielo.br)
  • Inherited haemoglobin disorders: an increasing global health problem. (who.int)
  • Management of birth defects and haemoglobin disorders : report of a joint WHO-March of Dimes meeting, Geneva, Switzerland, 17-19 May 2006. (who.int)
  • occurs when an abnormal hemoglobin S gene is inherited from both parents. (ms.gov)
  • occurs when an abnormal hemoglobin S gene is inherited from one parent and a hemoglobin C gene is inherited from the other parent. (ms.gov)
  • occurs when an abnormal hemoglobin S gene and a beta thalassemia gene are inherited. (ms.gov)
  • A new abnormal hemoglobin with instability and low oxygen affinity. (degruyter.com)
  • All babies born in Mississippi are tested for hemoglobin disease and trait. (ms.gov)
  • Most people with sickle cell trait do not have any health effects because they have some normal A hemoglobin. (ms.gov)
  • thalassemia major or thalassemia trait and hemoglobin E (HbE) are the second most common, 1 1 Wahed A, Quesada A, Dasgupta A. Hemoglobinopathies and Thalassemias. (scielo.br)
  • A retrospective study evaluated the impact of noninvasive and continuous hemoglobin monitoring using Masimo's SpHb on perioperative transfusion management and postoperative patient outcomes on pediatric patients undergoing fronto-orbital advancement surgery. (24x7mag.com)
  • Hemoglobin is a protein in red blood cells that carries oxygen. (medlineplus.gov)
  • A National Institutes of Health-funded study comparing low dose iron supplementation to no supplementation in blood donors found that supplementation significantly reduced the time to recovery of post-donation lost iron and hemoglobin-an iron-rich protein that carries oxygen in red blood cells throughout the body. (nih.gov)
  • Hemoglobin is a type of protein present in the RBCs that carries oxygen to the organs and transports carbon dioxide back to the lungs. (imarcgroup.com)
  • Hemoglobin C is an abnormal type of hemoglobin, the protein in red blood cells that carries oxygen. (stlukes-stl.com)
  • Within the first few months after birth, most babies have little to no fetal hemoglobin. (news-medical.net)
  • That is important for sickle cell because we know in adults that the fetal hemoglobin gene is shut down and we know fetal hemoglobin works very well as a disease modifier. (news-medical.net)
  • Two HDACs are involved in silencing the fetal hemoglobin gene and panobinostat is a pan-HDAC inhibitor, which means it silences more than one HDAC. (news-medical.net)
  • Hydroxyurea, the first sickle cell drug approved by the U.S. Food and Drug Administration back in 1998, also increases fetal hemoglobin, although precisely how remains unclear, and it's also used for some cancers. (news-medical.net)
  • Kutlar notes that if panobinostat continues to show promise, his next steps will include pairing the two fetal hemoglobin promoters to see if there is beneficial synergy. (news-medical.net)
  • The investigators will be monitoring study participants' levels of the non-sickling fetal hemoglobin as well as levels of F-cells, a subpopulation of red blood cells that contain fetal hemoglobin. (news-medical.net)
  • Pace has shown panobinostat increases fetal hemoglobin expression both in red blood cells in culture and in mouse models of sickle cell disease by enabling reactivation of the fetal hemoglobin gene. (news-medical.net)
  • What role does BPG play in transfer of oxygen from the maternal hemoglobin (HbA) to the fetal hemoglobin (HbF)? (flashcardmachine.com)
  • High hemoglobin level is most often caused by low oxygen levels in the blood (hypoxia), present over a long period of time. (medlineplus.gov)
  • A study by Holsen et al indicated that in women, recurrent major depressive disorder (MDD) influences hemoglobin A1c levels. (medscape.com)
  • Low hemoglobin levels often indicate anemia, but high levels can also be a sign of a serious health condition. (medicalnewstoday.com)
  • Read on to learn more about how hemoglobin levels can affect people, including symptoms, treatment, and outlook for someone with low hemoglobin in their body. (medicalnewstoday.com)
  • How are hemoglobin levels tested? (medicalnewstoday.com)
  • A blood test can assess hemoglobin levels. (medicalnewstoday.com)
  • Doctors may measure hemoglobin levels as part of a complete blood count (CBC) test. (medicalnewstoday.com)
  • In the United States, doctors diagnose anemia when the test finds hemoglobin levels to be less than 13.5 g/dL in males and less than 12.0 g/dL in females. (medicalnewstoday.com)
  • High hemoglobin levels could signal a rare blood disorder called polycythemia . (medicalnewstoday.com)
  • Low hemoglobin levels usually indicate that a person has anemia. (medicalnewstoday.com)
  • The results of a hemoglobin test will indicate if a person's hemoglobin levels are within the normal reference range. (medicalnewstoday.com)
  • Higher mean hemoglobin levels were observed among donors at higher altitudes for both males and females. (redcross.org)
  • Jean and I were amazed because it typically takes 2 to 3 weeks of supplements and other consistent efforts to even begin to see a change in hemoglobin levels. (emofree.com)
  • Hemoglobin Levels: What's Considered Normal? (healthline.com)
  • Typical hemoglobin levels vary depending on a number of individual factors. (healthline.com)
  • Older adults also tend to have lower hemoglobin levels. (healthline.com)
  • Infants tend to have higher average hemoglobin levels than adults . (healthline.com)
  • What causes high hemoglobin levels? (healthline.com)
  • High hemoglobin levels generally accompany high red blood cell counts. (healthline.com)
  • The 20 mothers who had hemoglobin levels below 10 g per dL (100 g per L) or a hematocrit level below 30 percent (0.30) at 26 to 28 weeks of gestation were provided with 325 mg per day of ferrous sulfate. (aafp.org)
  • This study highlights the importance of maintaining iron levels after blood donation, and shows that supplemental iron effectively restores hemoglobin, even in donors with higher iron levels," explained the study's principal investigator, Joseph Kiss, M.D., medical director at the Institute for Transfusion Medicine and associate professor of medicine, University of Pittsburgh. (nih.gov)
  • Hemoglobin and iron levels were measured seven times during the study. (nih.gov)
  • Compared to donors who did not take iron, the donors taking iron supplements returned to pre-donation hemoglobin levels faster in both the lower iron (five weeks versus 23 weeks) and higher iron groups (four weeks versus 11 weeks). (nih.gov)
  • Low hemoglobin levels lead to anemia, which causes symptoms like fatigue and trouble breathing. (meltingpointathens.com)
  • Testing Hemoglobin Levels. (meltingpointathens.com)
  • Symptoms Of High Hemoglobin Levels. (meltingpointathens.com)
  • Symptoms Of Conditions Associated With High Hemoglobin Levels. (meltingpointathens.com)
  • Hemoglobin levels are highly variable from person to person and may even shift within one person over the course of several days. (meltingpointathens.com)
  • Can we hold the injection for the time being & monitor haemoglobin levels? (ndtv.com)
  • For example, in patients whose records of fingerstick glucose are incomplete, reflecting good control in the week prior to a physician's visit, a hemoglobin A1c value of 6.8% is reassuring, whereas a value of 9.6% indicates that glucose levels were probably much higher in the preceding weeks. (medscape.com)
  • This case study examines a patient undergoing an elective procedure who had a past medical history of Hemoglobin Louisville and presented with baseline oxygen saturation levels ( SpO2 ) in the 80s as measured by noninvasive pulse oximetry . (bvsalud.org)
  • Free serum hemoglobin and haptoglobin levels are drawn to assess for hemolytic anemias. (cdc.gov)
  • Medical tests included blood lead levels, free erythrocyte-protoporphyrin (FEP), zinc protoporphyrin (ZPP), hemoglobin, and a chemistry profile. (cdc.gov)
  • Tests to measure haemoglobin levels are easy to administer. (who.int)
  • Hemoglobin has an oxygen-binding capacity of 1.34 mL O2 per gram, which increases the total blood oxygen capacity seventy-fold compared to dissolved oxygen in blood plasma alone. (wikipedia.org)
  • There are over 600 hemoglobin diseases that have been medically defined by the American College of Medical Genetics. (ms.gov)
  • In humans, hemoglobin A (the main form of hemoglobin in adults) is coded by genes HBA1, HBA2, and HBB. (wikipedia.org)
  • In a study on vertebrate globins, Jay Storz and his colleagues wrote, "The retention of the proto- Hb and Mb genes in the ancestor of jawed vertebrates permitted a physiological division of labor between the oxygen-carrier function of Hb [hemoglobin] and the oxygen-storage function of Mb [myoglobin]. (icr.org)
  • It is caused by homozygous inheritance of genes for hemoglobin. (msdmanuals.com)
  • The most common type of hemoglobin in mammals contains four such subunits. (wikipedia.org)
  • Structural study of hemoglobin Hazebrouck, beta 38(C4)Thr→Pro. (degruyter.com)
  • While the full physiological significance of the developmental diversity of hemoglobins is not yet understood, it is clear that the multiplicity of hemoglobins produced in a developmentally controlled manner is a strongly conserved feature across vertebrates, including the jawless vertebrates (agnathans), which are the most distantly related extant vertebrate relatives to humans. (icr.org)
  • The species for which myoglobin is used will cluster together far away from the related species for which hemoglobin is selected. (icr.org)
  • How many sub-units does myoglobin and hemoglobin have, respectively? (flashcardmachine.com)
  • Hemoglobin and hemoglobin-like molecules are also found in many invertebrates, fungi, and plants. (wikipedia.org)
  • In these organisms, hemoglobins may carry oxygen, or they may transport and regulate other small molecules and ions such as carbon dioxide, nitric oxide, hydrogen sulfide and sulfide. (wikipedia.org)
  • Each hemoglobin protein contains four iron atoms and can therefore carry four molecules of oxygen. (medicalnewstoday.com)
  • Scientists have no fossil molecules, and thus they cannot go back into deep evolutionary time and analyze the hypothetical pre-hemoglobin that supposedly existed. (icr.org)
  • Hemoglobin molecules consist of polypeptide chains whose chemical structure is genetically. (msdmanuals.com)
  • IMARC Group provides an analysis of the key trends in each sub-segment of the global hemoglobin testing market report, along with forecasts at the global and regional level from 2023-2028. (imarcgroup.com)
  • Mean hemoglobin concentrations, adjusted by sex, increased exponentially at altitudes above 11000 feet but the increase was less conspicuous at lower altitudes. (redcross.org)
  • By the time the women were admitted in labor, the mean hemoglobin and hematocrit values had increased by a mean of 0.5 g per dL (5 g per L) and 2.8 percent (0.03), respectively. (aafp.org)
  • Intensive glucose control in diabetic patients, reflected in lower hemoglobin A1c values, has been shown to "delay the onset and slow the progression of diabetic retinopathy, nephropathy, and neuropathy. (medscape.com)
  • Higher altitudes correlate with higher hemoglobin concentrations in healthy individuals when adjusted by other factors such age, race, and gender. (redcross.org)
  • and among subjects who achieved their randomized target, no increased risk associated with the higher hemoglobin goal was detected. (nih.gov)
  • As a result, the hemoglobin A1c level reflects the average blood glucose level over the course of the red blood cell's lifespan, roughly 120 days. (medscape.com)
  • In adults, the average hemoglobin level is slightly higher for men than it is for women . (healthline.com)
  • Unlike adults who have alpha and beta chains in the hemoglobin, a foetus expresses a zeta chain instead of alpha and epsilon, then later gamma instead of the HbA beta chain. (flashcardmachine.com)
  • Excessive glucose in the blood can attach to hemoglobin and raise the level of hemoglobin A1c. (wikipedia.org)
  • In those with both recurrent MDD and obesity, the hemoglobin A1c level was higher than in women with obesity but no recurrent MDD (5.75% vs 5.44%, respectively). (medscape.com)
  • A low level of hemoglobin in the blood means there is also a low level of oxygen. (medicalnewstoday.com)
  • While Chelle talked to Jean about her previous hemorrhages and her concern about bleeding too much after this birth, Jean tested Chelle's hemoglobin level. (emofree.com)
  • Then, intuitively, Jean asked Chelle the million dollar question: 'If there were an emotional reason for your low hemoglobin level, what might it be? (emofree.com)
  • The more fear Chelle felt, the lower her hemoglobin level might go, which would put her that much more at risk of a postpartum hemorrhage. (emofree.com)
  • Even though my hemoglobin level is low because I'm afraid I may bleed too much. (emofree.com)
  • Doctors determine your hemoglobin level by analyzing a sample of your blood. (healthline.com)
  • Keep reading to learn more about what's considered a normal, high, and low hemoglobin level. (healthline.com)
  • What's a normal hemoglobin level? (healthline.com)
  • Remember, hemoglobin is found in red blood cells, so the higher your red blood cell count, the higher your hemoglobin level and vice versa. (healthline.com)
  • A low hemoglobin level is usually seen with low red blood cell counts. (healthline.com)
  • We were unable to find reports in the published medical literature of any cases of bowel surgery being successfully performed at such a low hemoglobin level, without blood transfusion or blood products pre or post-surgery, with the patient's uncomplicated recovery. (wjgnet.com)
  • He had an extremely low hemoglobin level (2 g/dL) and mild renal and hepatic impairment. (wjgnet.com)
  • What is considered a low hemoglobin level? (meltingpointathens.com)
  • A low level of hemoglobin in the blood relates directly to a low level of oxygen. (meltingpointathens.com)
  • What level of hemoglobin is severe? (meltingpointathens.com)
  • What level of hemoglobin is dangerously low? (meltingpointathens.com)
  • What is the minimum level of hemoglobin required for survival? (meltingpointathens.com)
  • There is no one, standard minimum level of hemoglobin agreed upon in the medical community. (meltingpointathens.com)
  • Based on the available evidence, transfusion in the critically ill patient without active ischemic heart disease should generally be withheld until the hemoglobin level falls to 7 g/dl. (meltingpointathens.com)
  • A hemoglobin test measures the count of red blood cells (RBC) or the level of hemoglobin in the blood. (imarcgroup.com)
  • Serum free hemoglobin is a blood test that measures the level of free hemoglobin in the liquid part of the blood (the serum). (stlukes-stl.com)
  • Why is my mother's haemoglobin level falling inspite of taking Eprex? (ndtv.com)
  • Since the beginning she is taking Eprex 4000 injection to maintain her haemoglobin level. (ndtv.com)
  • Recently, my mother started experiencing a problem of low haemoglobin level (4.5 to 6.5). (ndtv.com)
  • The doctor is yet to diagnose the exact problem to reduce level of haemoglobin. (ndtv.com)
  • The mean haemoglobin level by Sahli's method and HCS differed significantly. (who.int)
  • Hemoglobin attaches to red blood cells and delivers oxygen throughout the body - everywhere that blood flows. (medicalnewstoday.com)
  • Glucose, also called blood sugar , circulates throughout your blood and attaches to hemoglobin. (healthline.com)
  • Hemoglobin has several other cysteines, but as seen in PDB entry 1buw , nitric oxide attaches preferentially to this one cysteine in each of the two beta chains. (rcsb.org)
  • 4 The worms have an amazing extracellular multi-hemoglobin system with one in the coelomic cavity (a fluid-filled body cavity) and two in the vascular (blood system) compartment. (icr.org)
  • Besides age, race, gender and general health, blood hemoglobin concentrations are also affected by altitude. (redcross.org)
  • Variations in average hemoglobin concentrations among healthy donors were also observed among donors of different (self-designated) races after adjusting for sex of the donor and the altitude. (redcross.org)
  • A limitation of hemoglobin A1c is that it does not provide any indication of the changes in glucose concentrations throughout the day, for which frequent glucose measurements are needed. (medscape.com)
  • to assess the effect of delayed clamping of the umbilical cord on hemoglobin concentrations in infants up to three months of age born to anemic and non anemic mothers. (bvsalud.org)
  • At approximately three months of age, 210 (64.6%) infants had their hemoglobin concentrations, socioeconomic, anthropometric and infant feeding practices collected. (bvsalud.org)
  • A few drops of blood obtained by a finger-stick can be used to assess haemoglobin concentrations in the field using a portable haemoglobinometer. (who.int)
  • Hemoglobin A1c provides information comparable to what might be provided by having frequent glucose values throughout the day over the course of 3 months. (medscape.com)
  • Sensitivity and specificity were reported to be 74% and 88%, respectively, with the investigators stating that the predictive value of hemoglobin A1c is comparable to that of an oral glucose tolerance test measurement of 2-hour plasma glucose. (medscape.com)
  • Many laboratories report a calculated eAG (estimated average glucose) along with every measured hemoglobin A1c, which is designed to facilitate communication with patients, as well as to help clinicians appreciate the degree of hyperglycemia the A1c represents. (medscape.com)
  • The prevalence and molecular basis of hemoglobinopathies in Cambodia.Hemoglobin. (who.int)
  • The prevalence of detectable hemoglobin (Hb) C in people in the. (msdmanuals.com)
  • Hemoglobins occur sporadically among the invertebrate phyla in no obvious [evolutionary branching] pattern. (icr.org)
  • Hemoglobin and hematocrit measurements are performed in almost all women admitted to a hospital in labor. (aafp.org)
  • They argued that the physiologic changes of pregnancy result in the lowest hemoglobin and hematocrit values at 26 to 28 weeks of gestation. (aafp.org)
  • In their study, they evaluated the ability of hemoglobin and hematocrit measurements at 26 to 28 weeks of gestation to predict values during labor. (aafp.org)
  • In these women, hemoglobin and hematocrit measurements were obtained on admission and at 26 to 28 weeks of gestation. (aafp.org)
  • In addition to gathering data on the pregnant women, the authors interviewed 31 obstetric specialists from the unit to identify the hemoglobin and hematocrit values at which patient management decisions would be affected. (aafp.org)
  • If hemoglobin and hematocrit values are acceptable at that time, retesting later in pregnancy is not necessary in low-risk pregnant women. (aafp.org)
  • The potential savings would be between $22 and $39 per patient, depending on whether hemoglobin and hematocrit measurements or a complete blood count is ordered. (aafp.org)
  • A decrease in haptoglobin can support a diagnosis of hemolytic anemia when seen with an increased reticulocyte count, decreased erythrocyte count, decreased hemoglobin and hematocrit. (cdc.gov)
  • The medical condition hemoglobinemia, a form of anemia, is caused by intravascular hemolysis, in which hemoglobin leaks from red blood cells into the blood plasma. (wikipedia.org)
  • An example of hemoglobin disease is sickle cell anemia. (ms.gov)
  • Hemoglobin (Hb) is screened before whole blood donation to protect donors from anemia. (nih.gov)
  • Hemoglobin C Disease Hemoglobin C disease is a hemoglobinopathy that causes symptoms of a hemolytic anemia. (msdmanuals.com)
  • A healthy human has 12 to 20 grams of hemoglobin in every 100 mL of blood. (wikipedia.org)
  • Tests usually express hemoglobin, or Hb, in grams per deciliter (g/dL) of blood. (medicalnewstoday.com)
  • A low hemoglobin count is generally defined as less than 13.2 grams of hemoglobin per deciliter (132 grams per liter) of blood for men and less than 11.6 grams per deciliter (116 grams per liter) for women. (meltingpointathens.com)
  • We did a secondary analysis of patients with chronic kidney disease enrolled in the Correction of Hemoglobin in the Outcomes in Renal Insufficiency trial to measure the potential for competing benefit and harm from achieved hemoglobin and epoetin dose trials. (nih.gov)
  • No Racial Differences in the Association of Glycated Hemoglobin With Kidney Disease and Cardiovascular Outcomes. (diabetesjournals.org)
  • For their retrospective, case-control study, they collected data for 42 pediatric patients with plagiocephaly or trigonocephaly who underwent surgery between 2018 and 2021, dividing them into a group of 16 patients whose perioperative PBM included noninvasive, continuous hemoglobin monitoring (SpHb group), and 26 patients who were managed conventionally (control group). (24x7mag.com)
  • Hemoglobin is the oxygen-carrying component of red blood cells, and with sickle cell disease it's inefficient at this fundamental role. (news-medical.net)
  • The investigators have early evidence that the drug, which is taken in pill form, should directly target the hemoglobin problem in sickle cell disease. (news-medical.net)
  • What mutation in hemoglobin causes sickle cell? (flashcardmachine.com)
  • The most common of these are the sickle cell mutation (HbS) and the haemoglobin E (HbE) mutation. (thalassaemia.org.cy)
  • Hemoglobin S-C disease is suspected in patients whose clinical features suggest sickle cell disease or whose red blood cells demonstrate sickling. (msdmanuals.com)
  • This function is so important that this cysteine (Cys93beta) is one of only three amino acids in hemoglobin conserved across all mammals and birds (along with two that position the heme). (rcsb.org)
  • The delayed cord clamping benefits the hemoglobin status of infants, especially those born to non anemic mothers. (bvsalud.org)
  • A typical cyanosis workup includes CBC with differential and peripheral blood smear, free serum hemoglobin and haptoglobin, ABGs and pulse oximetry. (cdc.gov)
  • Tests to rule out hemolysis include CBC with differential, reticulocyte count, peripheral blood smear, lactate dehydrogenase (LDH), bilirubin, serum haptoglobin, free serum hemoglobin and Heinz body preparation. (cdc.gov)
  • Only half of the patients with diabetes achieve a glycated hemoglobin A 1c (HbA 1c ) of less than 7% (1), despite the availability of effective antidiabetic therapy and clinical practice guidelines that are updated annually (2). (cdc.gov)
  • Rare unstable and low oxygen affinity haemoglobin variant, Hb Hazebrouck, detected on Sysmex XN-9000" Clinical Chemistry and Laboratory Medicine (CCLM) , vol. 60, no. 5, 2022, pp. e116-e118. (degruyter.com)
  • ABSTRACT This study compared the validity of the haemoglobin colour scale (HCS) and clinical signs in diagnosing anaemia against Sahli's haemoglobinometer method as the gold standard, and assessed the reliability of HCS. (who.int)
  • These data demonstrates that healthy donors from centers at higher altitudes have an average hemoglobin that is relatively greater than those from centers at lower altitudes. (redcross.org)
  • In mammals, hemoglobin makes up about 96% of a red blood cell's dry weight (excluding water), and around 35% of the total weight (including water). (wikipedia.org)
  • Nitric oxide, in bright blue and red, is attached to a specific cysteine in each of the beta chains of hemoglobin. (rcsb.org)
  • First, nitric oxide forms a complex with a specific cysteine on the beta chains of hemoglobin, binding preferentially to the oxygenated form. (rcsb.org)
  • A study by Vehik et al indicated that a rise in hemoglobin A1c of 10% or more from baseline signals an increased risk in pediatric patients of stage 3 type 1 diabetes mellitus, when other factors, including genetic risk and diabetes-associated autoantibodies, are also present. (medscape.com)
  • This is a genetic condition where the hemoglobin protein is abnormal. (medicalnewstoday.com)
  • The abundance, stability, and oxygen-carrying properties of hemoglobin can be altered by genetic mutations. (cshlpress.com)
  • Unstable hemoglobins: influence of environment on phenotypic expression of a genetic disorder. (degruyter.com)
  • Hemoglobin is an iron-containing oxygen-transport protein found in red blood cells. (icr.org)
  • The high molecular mass hemoglobin of the worm is the transporter for both oxygen and sulfide. (icr.org)
  • The high-resolution X-ray structures of the deoxy forms of four recombinant hemoglobins in which Trp37(C3)beta is replaced with Tyr (betaW37Y), Ala (betaW37A), Glu (betaW37E), or Gly (betaW37G) have been refined and analyzed with superposition methods that partition mutation-induced perturbations into quaternary structure changes and tertiary structure changes. (rcsb.org)
  • Structurally, what are the names of the deoxy and oxygenated forms of the hemoglobin respectively? (flashcardmachine.com)
  • D-2-3 Bisphosphoglycerate decreases the affinity hemoglobin for oxygen by binding to and stabilizing the deoxy-hemoglobin state. (flashcardmachine.com)
  • Dehydration, smoking , or living at high altitudes may also cause high hemoglobin. (medicalnewstoday.com)
  • In the 4 month analysis, significantly more patients in the high-hemoglobin compared to the low-hemoglobin arm were unable to achieve target hemoglobin and required high-dose epoetin-alpha. (nih.gov)
  • In unadjusted analyses, the inability to achieve a target hemoglobin and high-dose epoetin-alpha were each significantly associated with increased risk of a primary endpoint (death, myocardial infarction, congestive heart failure or stroke). (nih.gov)
  • In adjusted models, high-dose epoetin-alpha was associated with a significant increased hazard of a primary endpoint but the risk associated with randomization to the high hemoglobin arm did not suggest a possible mediating effect of higher target via dose. (nih.gov)
  • Causes For High Hemoglobin. (meltingpointathens.com)
  • Previously, the authors examined the UV-visible absorption spectral profile of hemoglobin (Hb) in dried bloodstains of different ages and identified a hypsochromic shift (blue shift, shift to shorter wavelength) of the HbSoret band that demonstrated a high correlation with TSD. (ojp.gov)
  • The global hemoglobin testing market size reached US$ 2.3 Billion in 2022. (imarcgroup.com)
  • Hemoglobin, the substance that gives color to red blood cells, is the substance that allows for the transport of oxygen throughout the body. (meltingpointathens.com)
  • Noting the frequency of significant hemorrhage during craniofacial reconstruction surgery, and the importance of an adequate patient blood management (PBM) policy during such surgery, the researchers sought to determine whether PBM that included noninvasive and continuous hemoglobin monitoring might improve transfusion management and outcomes for children undergoing frontal advancement surgery. (24x7mag.com)
  • This study adds outcomes evidence for pediatric patients to the growing literature on the value of continuous hemoglobin monitoring with SpHb. (24x7mag.com)
  • Saracoglu A, Abdullayez R, Sakar M, Sacak B, Incekoy F, Aykac Z. Continuous hemoglobin measurement during frontal advancement operations can improve patient outcomes. (24x7mag.com)
  • In 1851, German physiologist Otto Funke published a series of articles in which he described growing hemoglobin crystals by successively diluting red blood cells with a solvent such as pure water, alcohol or ether, followed by slow evaporation of the solvent from the resulting protein solution. (wikipedia.org)
  • The structure of S-nitrosylated hemoglobin (PDB entry 1buw ) was determined by starting with crystals of hemoglobin with carbon monoxide, and then exposing them to nitric oxide gas. (rcsb.org)