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.
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.
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.
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)
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.

The determination of hemoglobin and myoglogin residues as a parameter for testing heat exposure in back bacon. (1/8574)

The use of an extraction of the heme pigments hemoglobin and myoglobin as a test for the heat exposure of back bacon was investigated by treating back bacon at varying temperatures of 50-70 degrees C and times of two to 180 minutes and observing the effect on the absorbance of heme pigment residue after nitrite oxidation. Absorbance at 409 nm was used in place of the more usual 540 nm to provide greater sensitivity in the detection of heme. A decrease in residual heme pigments was time-dependent, particularly at lower temperatures. In view of this factor and the complex nature of the heat exposure of a large block of back bacon, the application of this test would require a calibration of each process. Alternatively, limits to the amounts of heme pigment residue could be set. The heme pigment test is useful in its simplicity and overcomes difficulties associated with the coagulation and enzyme tests.  (+info)

Thiamine deficiency is prevalent in a selected group of urban Indonesian elderly people. (2/8574)

This cross-sectional study involved 204 elderly individuals (93 males and 111 females). Subjects were randomly recruited using a list on which all 60-75 y-old-people living in seven sub-villages in Jakarta were included. The usual food intake was estimated using semiquantitative food frequency questionnaires. Hemoglobin, plasma retinol, vitamin B-12, red blood cell folate and the percentage stimulation of erythrocyte transketolase (ETK), as an indicator of thiamine status, were analyzed. Median energy intake was below the assessed requirement. More than 75% of the subjects had iron and thiamine intakes of approximately 2/3 of the recommended daily intake, and 20.2% of the study population had folate intake of approximately 2/3 of the recommended daily intake. Intakes of vitamins A and B-12 were adequate. Biochemical assessments demonstrated that 36.6% of the subjects had low thiamine levels (ETK stimulation > 25%). The elderly men tended to have lower thiamine levels than the elderly women. The overall prevalence of anemia was 28.9%, and the elderly women were affected more than the elderly men. Low biochemical status of vitamins A, B-12 and RBC folate was found in 5.4%, 8.8 % and 2.9% of the subjects, respectively. Dietary intakes of thiamine and folate were associated with ETK stimulation and plasma vitamin B-12 concentration (r = 0.176, P = 0.012 and r = 0.77, P = 0.001), respectively. Results of this study suggest that anemia, thiamine and possibly vitamin B-12 deficiency are prevalent in the elderly living in Indonesia. Clearly, micronutrient supplementation may be beneficial for the Indonesian elderly population living in underprivileged areas.  (+info)

Subunit dissociation in fish hemoglobins. (3/8574)

The tetramer-dimer dissociation equilibria (K 4,2) of several fish hemoglobins have been examined by sedimentation velocity measurements with a scanner-computer system for the ultracentrifuge and by flash photolysis measurements using rapid kinetic methods. Samples studied in detail included hemoglobins from a marine teleost, Brevoortia tyrannus (common name, menhaden); a fresh water teleost, Cyprinus carpio, (common name, carp); and an elasmobranch Prionace glauca (common name, blue shark). For all three species in the CO form at pH 7, in 0.1 M phosphate buffer, sedimentation coefficients of 4.3 S (typical of tetrameric hemoglobin) are observed in the micromolar concentration range. In contrast, mammalian hemoglobins dissociate appreciably to dimers under these conditions. The inability to detect dissociation in three fish hemoglobins at the lowest concentrations examined indicates that K 4,2 must have a value of 10(-8) M or less. In flash photolysis experiments on very dilute solutions in long path length cells, two kinetic components were detected with their proportions varying as expected for an equilibrium between tetramers (the slower component) and dimers (the faster component); values of K 4,2 for the three fish hemoglobins in the range 10(-9) to 10(-8) M were calculated from these data. Thus, the values of K 4,2 for liganded forms of the fish hemoglobins appear to be midway between the value for liganded human hemoglobin (K 4,2 approximately 10(-6) M) and unliganded human hemoglobin (K 4,2 approximately 10(-12) M). This conclusion is supported by measurements on solutions containing guanidine hydrochloride to enhance the degree of dissociation. All three fish hemoglobins are appreciably dissociated at guanidine concentrations of about 0.8 M, which is roughly midway between the guanidine concentrations needed to cause comparable dissociation of liganded human hemoglobin (about 0.4 M) and unliganded human hemoglobin (about 1.6 M). Kinetic measurements on solutions containing guanidine hydrochloride indicated that there are changes in both the absolute rates and the proportions of the fast and slow components, which along with other factors complicated the analysis of the data in terms of dissociation constants. Measurements were also made in solutions containing urea to promote dissociation, but with this agent very high concentrations (about 6 M) were required to give measureable dissociation and the fish hemoglobins were unstable under these conditions, with appreciable loss of absorbance spectra in both the sedimentation and kinetic experiments.  (+info)

Reactivity of cyanate with valine-1 (alpha) of hemoglobin. A probe of conformational change and anion binding. (4/8574)

The 3-fold increase in the carbamylation rate of Val-1 (alpha) of hemoglobin upon deoxygenation described earlier is now shown to be a sensitive probe of conformational change. Thus, whereas this residue in methemoglobin A is carbamylated at the same rate as in liganded hemoglobin, upon addition of inositol hexaphosphate its carbamylation rate is enhanced 30% as much as the total change in the rate between the CO and deoxy states. For CO-hemoglobin Kansas in the presence of the organic phosphate, the relative increase in the carbamylation rate of this residue is about 50%. These results indicate that methemoglobin A and hemoglobin Kansas in the presence of inositol hexaphosphate do not assume a conformation identical with deoxyhemoglobin but rather form either a mixture of R and T states or an intermediate conformation in the region around Val-1 (alpha). Studies on the mechanism for the rate enhancement in deoxyhemoglobin suggest that the cyanate anion binds to groups in the vicinity of Val-1 (alpha) prior to proton transfer and carbamylation of this NH2-terminal residue. Thus, specific removal with carboxypeptidase B of Arg-141 (alpha), which is close to Val-1 (alpha) in deoxyhemoglobin, abolishes the enhancement in carbamylation. Chloride, which has the same valency as cyanate, is a better competitive inhibitor of the carbamylation of deoxyhemoglobin (Ki = 50 mM) compared with liganded hemoglobin. Nitrate and iodide are also effective inhibitors of the carbamylation of Val-1 (alpha) of deoxyhemoglobin (Ki = 35 mM); inorganic phosphate, sulfate, and fluoride are poor competitive inhibitors. The change in pKa of Val-1 (alpha) upon deoxygenation may be due to its differential interaction with chloride.  (+info)

Aggregation of deoxyhemoglobin S at low concentrations. (5/8574)

The self-association of deoxyhemoglobin S was measured in dilute solutions (0 to 5 g/dl) by Rayleigh light scattering at 630 nm and osmometry in 0.05 M potassium phosphate buffer (pH 7.35). Weight and number average molecular weights (Mw and Mn, respectively) and the second or higher virial coefficients, B' were determined. No experimentally significant differences were observed between oxy- and deoxy-Hb S up to the concentration of 2 g/dl; their apparent average molecular weights were within experimental error. Above that concentration, both Mn and Mw of deoxy-Hb S were significantly different from that of oxy-Hb S. The negative second viral coefficent of deoxy-Hb S, observed by both techniques, is consistent with the self-association of this protein. The lack of effect of 0.4 M propylurea on the state of aggregation and the significant influence of 0.1 M NaCl suggests that polar interactions are involved in formation of these aggregates.  (+info)

O-raffinose cross-linking markedly reduces systemic and renal vasoconstrictor effects of unmodified human hemoglobin. (6/8574)

The hemodynamic effects of a 20% exchange-transfusion with different solutions of highly purified human hemoglobin A-zero (A0) were evaluated. We compared unmodified hemoglobin with hemoglobin cross-linked with O-raffinose. Unmodified hemoglobin increased systemic vascular resistance and mean arterial pressure more than the O-raffinose cross-linked hemoglobin solution (by approximately 45% and approximately 14%, respectively). Unmodified hemoglobin markedly reduced cardiac output (CO) by approximately 21%, whereas CO was unaffected by the O-raffinose cross-linked hemoglobin solution. Unmodified and O-raffinose cross-linked hemoglobin solutions increased mean arterial pressure to comparable extents ( approximately 14% and approximately 9%, respectively). Unmodified hemoglobin increased renal vascular resistance 2-fold and reduced the glomerular filtration rate by 58%. In marked contrast, the O-raffinose cross-linked hemoglobin had no deleterious effect on the glomerular filtration rate, renal blood flow, or renal vascular resistance. The extents to which unmodified and O-raffinose cross-linked hemoglobin solutions inactivated nitric oxide also were compared using three separate in vitro assays: platelet nitric oxide release, nitric oxide-stimulated platelet cGMP production, and endothelium-derived relaxing factor-mediated inhibition of platelet aggregation. Unmodified hemoglobin inactivated or oxidized nitric oxide to a greater extent than the O-raffinose cross-linked hemoglobin solutions in all three assays. In summary, O-raffinose cross-linking substantially reduced the systemic vasoconstriction and the decrease in CO induced by unmodified hemoglobin and eliminated the deleterious effects of unmodified hemoglobin on renal hemodynamics and function. We hypothesize that O-raffinose cross-linking reduces the degree of oxidation of nitric oxide and that this contributes to the reduced vasoactivity of this modified hemoglobin.  (+info)

Detection of viruses and body fluids which may contain viruses in the domestic environment. (7/8574)

The domestic environment was investigated for the presence of viruses and body fluids that may contain viruses. A range of surfaces in 39 homes (17 visited on 2 occasions) were sampled by swabbing and analysed using cell culture, reverse transcription polymerase chain reaction for enteroviral RNA, haemoglobin as a marker for blood, amylase as an indicator of urine, saliva and sweat, and protein as an indicator of general hygiene. Haemoglobin was found on 1.9% of surfaces sampled and of the positive samples 30% were from articles frequently handled. Amylase (> 5 U/l) was found in 29.3% of samples tested. Protein was found in 97.8% of samples tested. Enteroviral RNA, indicating the presence of virus, was detected in 3 out of 448 samples tested; they were from a tap handle, telephone handpiece and a toilet bowl. No viruses were isolated in cell culture, however significant problems were encountered with bacterial and fungal contamination. This work demonstrates that only testing environmental samples for bacteria and ATP may not give a total view of the microbiological problem in the home. A range of test methods is useful to gain a broad view of the problems of hygiene in the home and to allow comparative studies of specific areas such as the kitchen and bathroom.  (+info)

Amino acid sequences of the alpha and beta chains of adult hemoglobin of the slender loris, Loris tardigradus. (8/8574)

alpha and beta chains from adult hemoglobin of the slender loris (Loris tardigradus) were isolated by Amberlite CG-50 column chromatography. After S-aminoethylation, both chains were digested with trypsin and the amino acid sequences of the tryptic peptides obtained were analyzed. Further, the order of these tryptic peptides in each chain was deduced from their homology with the primary structures of alpha and beta chains of human adult hemoglobin. Comparing the primary structures of the alpha and beta chains of adult hemoglobin of the slender loris thus obtained with those of adult hemoglobin of the slow loris, 4 amino acid substitutions in the alpha chains and 2 in the beta chains were recognized.  (+info)

There are many different types of anemia, each with its own set of causes and symptoms. Some common types of anemia include:

1. Iron-deficiency anemia: This is the most common type of anemia and is caused by a lack of iron in the diet or a problem with the body's ability to absorb iron. Iron is essential for making hemoglobin.
2. Vitamin deficiency anemia: This type of anemia is caused by a lack of vitamins, such as vitamin B12 or folate, that are necessary for red blood cell production.
3. Anemia of chronic disease: This type of anemia is seen in people with chronic diseases, such as kidney disease, rheumatoid arthritis, and cancer.
4. Sickle cell anemia: This is a genetic disorder that affects the structure of hemoglobin and causes red blood cells to be shaped like crescents or sickles.
5. Thalassemia: This is a genetic disorder that affects the production of hemoglobin and can cause anemia, fatigue, and other health problems.

The symptoms of anemia can vary depending on the type and severity of the condition. Common symptoms include fatigue, weakness, pale skin, shortness of breath, and dizziness or lightheadedness. Anemia can be diagnosed with a blood test that measures the number and size of red blood cells, as well as the levels of hemoglobin and other nutrients.

Treatment for anemia depends on the underlying cause of the condition. In some cases, dietary changes or supplements may be sufficient to treat anemia. For example, people with iron-deficiency anemia may need to increase their intake of iron-rich foods or take iron supplements. In other cases, medical treatment may be necessary to address underlying conditions such as kidney disease or cancer.

Preventing anemia is important for maintaining good health and preventing complications. To prevent anemia, it is important to eat a balanced diet that includes plenty of iron-rich foods, vitamin C-rich foods, and other essential nutrients. It is also important to avoid certain substances that can interfere with the absorption of nutrients, such as alcohol and caffeine. Additionally, it is important to manage any underlying medical conditions and seek medical attention if symptoms of anemia persist or worsen over time.

In conclusion, anemia is a common blood disorder that can have significant health implications if left untreated. It is important to be aware of the different types of anemia, their causes, and symptoms in order to seek medical attention if necessary. With proper diagnosis and treatment, many cases of anemia can be successfully managed and prevented.

The most common types of hemoglobinopathies include:

1. Sickle cell disease: This is caused by a point mutation in the HBB gene that codes for the beta-globin subunit of hemoglobin. It results in the production of sickle-shaped red blood cells, which can cause anemia, infections, and other complications.
2. Thalassemia: This is a group of genetic disorders that affect the production of hemoglobin and can result in anemia, fatigue, and other complications.
3. Hemophilia A: This is caused by a defect in the F8 gene that codes for coagulation factor VIII, which is essential for blood clotting. It can cause bleeding episodes, especially in males.
4. Glucose-6-phosphate dehydrogenase (G6PD) deficiency: This is caused by a point mutation in the G6PD gene that codes for an enzyme involved in red blood cell production. It can cause hemolytic anemia, especially in individuals who consume certain foods or medications.
5. Hereditary spherocytosis: This is caused by point mutations in the ANK1 or SPTA1 genes that code for proteins involved in red blood cell membrane structure. It can cause hemolytic anemia and other complications.

Hemoglobinopathies can be diagnosed through genetic testing, such as DNA sequencing or molecular genetic analysis. Treatment options vary depending on the specific disorder but may include blood transfusions, medications, and in some cases, bone marrow transplantation.

Hemoglobin C disease is characterized by the presence of both normal hemoglobin (HbA) and abnormal hemoglobin (HbC) in red blood cells, which leads to a variety of symptoms and complications. The severity of the disease can range from mild to severe, depending on the specific mutations present and the percentage of HbC in the blood.

Symptoms of Hemoglobin C Disease:

The symptoms of hemoglobin C disease can vary in severity and may include:

1. Anemia: People with HbC disease often have lower than normal levels of red blood cells, which can lead to fatigue, weakness, and shortness of breath.
2. Jaundice: Yellowing of the skin and eyes due to high bilirubin levels can occur in severe cases of HbC disease.
3. Enlarged spleen: The spleen may become enlarged due to the accumulation of abnormal red blood cells.
4. Gallstones: People with HbC disease are at increased risk of developing gallstones.
5. Pain: Pain in the abdomen, joints, and other parts of the body can occur due to the abnormal hemoglobin.
6. Increased risk of infections: People with HbC disease may be more susceptible to infections due to their anemia and weakened immune system.
7. Delayed development: Children with HbC disease may experience delayed development and growth.

Complications of Hemoglobin C Disease:

Hemoglobin C disease can lead to a number of complications, including:

1. Stroke: People with HbC disease are at increased risk of stroke due to the abnormal hemoglobin.
2. Heart failure: The heart may become enlarged and fail to pump blood effectively due to the strain placed on it by the abnormal red blood cells.
3. Kidney damage: The kidneys may be damaged due to the accumulation of abnormal red blood cells.
4. Anemia: People with HbC disease may develop anemia, which can lead to fatigue, weakness, and shortness of breath.
5. Blood transfusions: Regular blood transfusions may be necessary to maintain healthy red blood cell levels.
6. Iron overload: The frequent blood transfusions can lead to iron overload, which can cause liver damage and other complications.
7. Increased risk of cancer: People with HbC disease may be at increased risk of developing certain types of cancer, such as leukemia.
8. Increased risk of thrombosis: The abnormal hemoglobin can increase the risk of blood clots and thrombosis.
9. Shortened lifespan: People with HbC disease may have a shorter lifespan compared to those without the condition.
10. Reduced quality of life: HbC disease can significantly impact an individual's quality of life, leading to fatigue, pain, and other symptoms that can affect daily activities and relationships.

It is important to note that these complications can be managed with proper medical care and attention. Regular monitoring and follow-up with a healthcare provider are crucial for managing the disease and preventing or minimizing these complications.

Sickle cell anemia is caused by mutations in the HBB gene that codes for hemoglobin. The most common mutation is a point mutation at position 6, which replaces the glutamic acid amino acid with a valine (Glu6Val). This substitution causes the hemoglobin molecule to be unstable and prone to forming sickle-shaped cells.

The hallmark symptom of sickle cell anemia is anemia, which is a low number of healthy red blood cells. People with the condition may also experience fatigue, weakness, jaundice (yellowing of the skin and eyes), infections, and episodes of severe pain. Sickle cell anemia can also increase the risk of stroke, heart disease, and other complications.

Sickle cell anemia is diagnosed through blood tests that measure hemoglobin levels and the presence of sickle cells. Treatment typically involves managing symptoms and preventing complications with medications, blood transfusions, and antibiotics. In some cases, bone marrow transplantation may be recommended.

Prevention of sickle cell anemia primarily involves avoiding the genetic mutations that cause the condition. This can be done through genetic counseling and testing for individuals who have a family history of the condition or are at risk of inheriting it. Prenatal testing is also available for pregnant women who may be carriers of the condition.

Overall, sickle cell anemia is a serious genetic disorder that can significantly impact quality of life and life expectancy if left untreated. However, with proper management and care, individuals with the condition can lead fulfilling lives and manage their symptoms effectively.

There are two main types of thalassemia: alpha-thalassemia and beta-thalassemia. Alpha-thalassemia is caused by abnormalities in the production of the alpha-globin chain, which is one of the two chains that make up hemoglobin. Beta-thalassemia is caused by abnormalities in the production of the beta-globin chain.

Thalassemia can cause a range of symptoms, including anemia, fatigue, pale skin, and shortness of breath. In severe cases, it can lead to life-threatening complications such as heart failure, liver failure, and bone deformities. Thalassemia is usually diagnosed through blood tests that measure the levels of hemoglobin and other proteins in the blood.

There is no cure for thalassemia, but treatment can help manage the symptoms and prevent complications. Treatment may include blood transfusions, folic acid supplements, and medications to reduce the severity of anemia. In some cases, bone marrow transplantation may be recommended.

Preventive measures for thalassemia include genetic counseling and testing for individuals who are at risk of inheriting the disorder. Prenatal testing is also available for pregnant women who are carriers of the disorder. In addition, individuals with thalassemia should avoid marriage within their own family or community to reduce the risk of passing on the disorder to their children.

Overall, thalassemia is a serious and inherited blood disorder that can have significant health implications if left untreated. However, with proper treatment and management, individuals with thalassemia can lead fulfilling lives and minimize the risk of complications.

The disease is classified into two main types: Hemoglobin SC disease and Hemoglobin SE disease. Hemoglobin SC disease is the most common type of hemoglobinopathy and affects approximately 1 in 10,000 people worldwide. It is more common in certain ethnic groups, such as people of African, Mediterranean, and Southeast Asian descent.

Hemoglobin SC disease can cause a range of symptoms, including anemia, fatigue, jaundice, and infections. The disease can also lead to complications such as splenomegaly (enlargement of the spleen), gallstones, and heart problems. Treatment for Hemoglobin SC disease typically involves blood transfusions and management of related complications.

In summary, Hemoglobin SC disease is a genetic disorder that affects the production of hemoglobin and can cause a range of symptoms and complications. It is more common in certain ethnic groups and can be managed with blood transfusions and other treatments.

Prevalence: Iron deficiency anemia is one of the most common nutritional disorders worldwide, affecting approximately 1.6 billion people, with women being more likely to be affected than men.

Causes: The main cause of iron deficiency anemia is a diet that does not provide enough iron. Other causes include:

* Poor absorption of iron from the diet
* Increased demand for iron due to growth or pregnancy
* Blood loss due to menstruation, internal bleeding, or surgery
* Chronic diseases such as kidney disease, cancer, and rheumatoid arthritis

Signs and symptoms: The signs and symptoms of iron deficiency anemia may include:

* Fatigue and weakness
* Pale skin
* Shortness of breath
* Dizziness or lightheadedness
* Headaches
* Cold hands and feet

Diagnosis: Iron deficiency anemia is diagnosed based on a physical exam, medical history, and laboratory tests, including:

* Complete blood count (CBC) to check for low red blood cell count and low hemoglobin level
* Serum iron and transferrin tests to check for low iron levels
* Ferritin test to check for low iron stores

Treatment: Treatment of iron deficiency anemia involves correcting the underlying cause, which may include:

* Dietary changes to increase iron intake
* Iron supplements to replenish iron stores
* Addressing any underlying causes such as bleeding or malabsorption

Complications: Iron deficiency anemia can lead to complications such as:

* Heart failure
* Increased risk of infections
* Poor cognitive function and development in children

Prevention: Preventing iron deficiency anemia involves consuming enough iron through a balanced diet, avoiding foods that inhibit iron absorption, and addressing any underlying causes. It is also important to maintain good overall health, including managing chronic conditions such as bleeding or malabsorption.

There are two main types of beta-thalassemia:

1. Beta-thalassemia major (also known as Cooley's anemia): This is the most severe form of the condition, and it can cause serious health problems and a shortened lifespan if left untreated. Children with this condition are typically diagnosed at birth or in early childhood, and they may require regular blood transfusions and other medical interventions to manage their symptoms and prevent complications.
2. Beta-thalassemia minor (also known as thalassemia trait): This is a milder form of the condition, and it may not cause any noticeable symptoms. People with beta-thalassemia minor have one mutated copy of the HBB gene and one healthy copy, which allows them to produce some normal hemoglobin. However, they may still be at risk for complications such as anemia, fatigue, and a higher risk of infections.

The symptoms of beta-thalassemia can vary depending on the severity of the condition and the age of onset. Common symptoms include:

* Fatigue
* Weakness
* Pale skin
* Shortness of breath
* Frequent infections
* Yellowing of the skin and eyes (jaundice)
* Enlarged spleen

Beta-thalassemia is most commonly found in people of Mediterranean, African, and Southeast Asian ancestry. It is caused by mutations in the HBB gene, which is inherited from one's parents. There is no cure for beta-thalassemia, but it can be managed with blood transfusions, chelation therapy, and other medical interventions. Bone marrow transplantation may also be a viable option for some patients.

In conclusion, beta-thalassemia is a genetic disorder that affects the production of hemoglobin, leading to anemia, fatigue, and other complications. While there is no cure for the condition, it can be managed with medical interventions and bone marrow transplantation may be a viable option for some patients. Early diagnosis and management are crucial in preventing or minimizing the complications of beta-thalassemia.

Sickle cell trait is relatively common in certain populations, such as people of African, Mediterranean, or Middle Eastern descent. It is estimated that about 1 in 12 African Americans carry the sickle cell gene, and 1 in 500 are homozygous for the trait (meaning they have two copies of the sickle cell gene).

Although people with sickle cell trait do not develop sickle cell anemia, they can experience certain complications related to the trait. For example, they may experience episodes of hemolytic crisis, which is a condition in which red blood cells are destroyed faster than they can be replaced. This can occur under certain conditions, such as dehydration or infection.

There are several ways that sickle cell trait can affect an individual's life. For example, some people with the trait may experience discrimination or stigma based on their genetic status. Additionally, individuals with sickle cell trait may be more likely to experience certain health problems, such as kidney disease or eye damage, although these risks are generally low.

There is no cure for sickle cell trait, but it can be managed through proper medical care and self-care. Individuals with the trait should work closely with their healthcare provider to monitor their health and address any complications that arise.

Overall, sickle cell trait is a relatively common genetic condition that can have significant implications for an individual's life. It is important for individuals with the trait to understand their risk factors and take steps to manage their health and well-being.

There are two main forms of alpha-Thalassemia:

1. Alpha-thalassemia major (also known as Hemoglobin Bart's hydrops fetalis): This is a severe form of the disorder that can cause severe anemia, enlarged spleen, and death in infancy. It is caused by a complete absence of one or both of the HBA1 or HBA2 genes.
2. Alpha-thalassemia minor (also known as Hemoglobin carrier state): This form of the disorder is milder and may not cause any symptoms at all. It is caused by a partial deletion of one or both of the HBA1 or HBA2 genes.

People with alpha-thalassemia minor may have slightly lower levels of hemoglobin and may be more susceptible to anemia, but they do not typically experience any severe symptoms. Those with alpha-thalassemia major, on the other hand, are at risk for serious complications such as anemia, infections, and organ failure.

There is no cure for alpha-thalassemia, but treatment options include blood transfusions, iron chelation therapy, and management of associated complications. Screening for alpha-thalassemia is recommended for individuals who are carriers of the disorder, as well as for those who have a family history of the condition.

There are two main types of hemolysis:

1. Intravascular hemolysis: This type occurs within the blood vessels and is caused by factors such as mechanical injury, oxidative stress, and certain infections.
2. Extravascular hemolysis: This type occurs outside the blood vessels and is caused by factors such as bone marrow disorders, splenic rupture, and certain medications.

Hemolytic anemia is a condition that occurs when there is excessive hemolysis of RBCs, leading to a decrease in the number of healthy red blood cells in the body. This can cause symptoms such as fatigue, weakness, pale skin, and shortness of breath.

Some common causes of hemolysis include:

1. Genetic disorders such as sickle cell anemia and thalassemia.
2. Autoimmune disorders such as autoimmune hemolytic anemia (AIHA).
3. Infections such as malaria, babesiosis, and toxoplasmosis.
4. Medications such as antibiotics, nonsteroidal anti-inflammatory drugs (NSAIDs), and blood thinners.
5. Bone marrow disorders such as aplastic anemia and myelofibrosis.
6. Splenic rupture or surgical removal of the spleen.
7. Mechanical injury to the blood vessels.

Diagnosis of hemolysis is based on a combination of physical examination, medical history, and laboratory tests such as complete blood count (CBC), blood smear examination, and direct Coombs test. Treatment depends on the underlying cause and may include supportive care, blood transfusions, and medications to suppress the immune system or prevent infection.

In hypochromic anemia, the RBCs are smaller than normal and have a lower concentration of hemoglobin. This can lead to a decrease in the amount of oxygen being carried to the body's tissues, which can cause fatigue, weakness, and shortness of breath.

There are several possible causes of hypochromic anemia, including:

1. Iron deficiency: Iron is essential for the production of hemoglobin, so a lack of iron can lead to a decrease in hemoglobin levels and the development of hypochromic anemia.
2. Vitamin deficiency: Vitamins such as vitamin B12 and folate are important for the production of red blood cells, so a deficiency in these vitamins can lead to hypochromic anemia.
3. Chronic disease: Certain chronic diseases, such as kidney disease, rheumatoid arthritis, and cancer, can lead to hypochromic anemia.
4. Inherited disorders: Certain inherited disorders, such as thalassemia and sickle cell anemia, can cause hypochromic anemia.
5. Autoimmune disorders: Autoimmune disorders, such as autoimmune hemolytic anemia, can cause hypochromic anemia by destroying red blood cells.

Hypochromic anemia is typically diagnosed through a combination of physical examination, medical history, and laboratory tests such as complete blood counts (CBCs) and serum iron studies. Treatment depends on the underlying cause of the anemia and may include dietary changes, supplements, medication, or blood transfusions.

Hemoglobinuria can be caused by a variety of factors, including:

1. Blood disorders such as sickle cell disease, thalassemia, and von Willebrand disease.
2. Inherited genetic disorders such as hemophilia.
3. Autoimmune disorders such as autoimmune hemolytic anemia.
4. Infections such as septicemia or meningococcemia.
5. Toxins such as lead, which can damage red blood cells and cause hemoglobinuria.
6. Certain medications such as antibiotics and nonsteroidal anti-inflammatory drugs (NSAIDs).
7. Kidney disease or failure.
8. Transfusion-related acute lung injury (TRALI), which can occur after blood transfusions.
9. Hemolytic uremic syndrome (HUS), a condition that occurs when red blood cells are damaged and broken down, leading to kidney failure.

The symptoms of hemoglobinuria may include:

1. Red or brown-colored urine
2. Frequent urination
3. Pale or yellowish skin
4. Fatigue
5. Shortness of breath
6. Nausea and vomiting
7. Headache
8. Dizziness or lightheadedness
9. Confusion or loss of consciousness in severe cases.

Diagnosis of hemoglobinuria is typically made through urine testing, such as a urinalysis, which can detect the presence of hemoglobin in the urine. Additional tests may be ordered to determine the underlying cause of hemoglobinuria, such as blood tests, imaging studies, or biopsies.

Treatment of hemoglobinuria depends on the underlying cause and severity of the condition. In some cases, treatment may involve addressing the underlying condition that is causing the hemoglobinuria, such as managing an infection or stopping certain medications. Other treatments may include:

1. Fluid and electrolyte replacement to prevent dehydration and maintain proper fluid balance.
2. Medications to help remove excess iron from the body.
3. Blood transfusions to increase the number of red blood cells in the body and improve oxygen delivery.
4. Dialysis to filter waste products from the blood when the kidneys are unable to do so.
5. Supportive care, such as oxygen therapy and pain management.

In severe cases of hemoglobinuria, complications can include:

1. Kidney damage or failure
2. Septicemia (blood infection)
3. Respiratory failure
4. Heart problems
5. Increased risk of infections and other complications.

Prevention of hemoglobinuria involves managing any underlying medical conditions, such as diabetes or infections, and avoiding certain medications that can cause the condition. It is also important to seek medical attention if symptoms of hemoglobinuria develop, as early treatment can help prevent complications and improve outcomes.

There are three main types of polycythemia:

1. Polycythemia vera (PV): This is the most common type and is characterized by an overproduction of red blood cells, white blood cells, and platelets. It is a slowly progressing disease that can lead to complications such as blood clots, bleeding, and an increased risk of cancer.
2. Essential thrombocythemia (ET): This type is characterized by an overproduction of platelets, which can increase the risk of blood clots and other cardiovascular problems.
3. Primary myelofibrosis (PMF): This type is characterized by bone marrow scarring, anemia, fatigue, and an increased risk of blood clots.

Symptoms of polycythemia may include:

* Headache
* Dizziness
* Fatigue
* Shortness of breath
* Pale skin
* Swelling in the spleen or liver

Diagnosis is based on a physical examination, medical history, and laboratory tests such as complete blood counts (CBCs) and bone marrow biopsies. Treatment options for polycythemia include:

1. Phlebotomy (removal of blood): This is the most common treatment for PV and ET, which involves removing excess blood to reduce the number of red blood cells, white blood cells, and platelets.
2. Chemotherapy: This may be used in combination with phlebotomy to treat PV and PMF.
3. Hydroxyurea: This medication is used to reduce the production of blood cells and relieve symptoms such as headache and dizziness.
4. Interferons: These medications are used to treat ET and may be effective in reducing the number of platelets.
5. Stem cell transplantation: In severe cases of PV or PMF, a stem cell transplant may be necessary.

It is important to note that these treatments do not cure polycythemia, but they can help manage symptoms and slow the progression of the disease. Regular monitoring and follow-up with a healthcare provider is essential to ensure the best possible outcomes.

1. Iron deficiency anemia: This is the most common hematologic complication of pregnancy, caused by the increased demand for iron and the potential for poor dietary intake or gastrointestinal blood loss.
2. Thrombocytopenia: A decrease in platelet count, which can be mild and resolve spontaneously or severe and require treatment.
3. Leukemia: Rare but potentially serious, leukemia can occur during pregnancy and may require prompt intervention to ensure the health of both the mother and the fetus.
4. Thrombosis: The formation of a blood clot in a blood vessel, which can be life-threatening for both the mother and the baby if left untreated.
5. Hemorrhage: Excessive bleeding during pregnancy, which can be caused by various factors such as placenta previa or abruption.
6. Preeclampsia: A condition characterized by high blood pressure and damage to organs such as the kidneys and liver, which can increase the risk of hemorrhage and other complications.
7. Ectopic pregnancy: A pregnancy that develops outside of the uterus, often in the fallopian tube, which can cause severe bleeding and be life-threatening if left untreated.

There are several types of diabetes mellitus, including:

1. Type 1 DM: This is an autoimmune condition in which the body's immune system attacks and destroys the cells in the pancreas that produce insulin, resulting in a complete deficiency of insulin production. It typically develops in childhood or adolescence, and patients with this condition require lifelong insulin therapy.
2. Type 2 DM: This is the most common form of diabetes, accounting for around 90% of all cases. It is caused by a combination of insulin resistance (where the body's cells do not respond properly to insulin) and impaired insulin secretion. It is often associated with obesity, physical inactivity, and a diet high in sugar and unhealthy fats.
3. Gestational DM: This type of diabetes develops during pregnancy, usually in the second or third trimester. Hormonal changes and insulin resistance can cause blood sugar levels to rise, putting both the mother and baby at risk.
4. LADA (Latent Autoimmune Diabetes in Adults): This is a form of type 1 DM that develops in adults, typically after the age of 30. It shares features with both type 1 and type 2 DM.
5. MODY (Maturity-Onset Diabetes of the Young): This is a rare form of diabetes caused by genetic mutations that affect insulin production. It typically develops in young adulthood and can be managed with lifestyle changes and/or medication.

The symptoms of diabetes mellitus can vary depending on the severity of the condition, but may include:

1. Increased thirst and urination
2. Fatigue
3. Blurred vision
4. Cuts or bruises that are slow to heal
5. Tingling or numbness in hands and feet
6. Recurring skin, gum, or bladder infections
7. Flu-like symptoms such as weakness, dizziness, and stomach pain
8. Dark, velvety skin patches (acanthosis nigricans)
9. Yellowish color of the skin and eyes (jaundice)
10. Delayed healing of cuts and wounds

If left untreated, diabetes mellitus can lead to a range of complications, including:

1. Heart disease and stroke
2. Kidney damage and failure
3. Nerve damage (neuropathy)
4. Eye damage (retinopathy)
5. Foot damage (neuropathic ulcers)
6. Cognitive impairment and dementia
7. Increased risk of infections and other diseases, such as pneumonia, gum disease, and urinary tract infections.

It is important to note that not all individuals with diabetes will experience these complications, and that proper management of the condition can greatly reduce the risk of developing these complications.

Type 2 diabetes can be managed through a combination of diet, exercise, and medication. In some cases, lifestyle changes may be enough to control blood sugar levels, while in other cases, medication or insulin therapy may be necessary. Regular monitoring of blood sugar levels and follow-up with a healthcare provider are important for managing the condition and preventing complications.

Common symptoms of type 2 diabetes include:

* Increased thirst and urination
* Fatigue
* Blurred vision
* Cuts or bruises that are slow to heal
* Tingling or numbness in the hands and feet
* Recurring skin, gum, or bladder infections

If left untreated, type 2 diabetes can lead to a range of complications, including:

* Heart disease and stroke
* Kidney damage and failure
* Nerve damage and pain
* Eye damage and blindness
* Foot damage and amputation

The exact cause of type 2 diabetes is not known, but it is believed to be linked to a combination of genetic and lifestyle factors, such as:

* Obesity and excess body weight
* Lack of physical activity
* Poor diet and nutrition
* Age and family history
* Certain ethnicities (e.g., African American, Hispanic/Latino, Native American)
* History of gestational diabetes or delivering a baby over 9 lbs.

There is no cure for type 2 diabetes, but it can be managed and controlled through a combination of lifestyle changes and medication. With proper treatment and self-care, people with type 2 diabetes can lead long, healthy lives.

Symptoms of hemolytic anemia may include fatigue, weakness, shortness of breath, dizziness, headaches, and pale or yellowish skin. Treatment options depend on the underlying cause but may include blood transfusions, medication to suppress the immune system, antibiotics for infections, and removal of the spleen (splenectomy) in severe cases.

Prevention strategies for hemolytic anemia include avoiding triggers such as certain medications or infections, maintaining good hygiene practices, and seeking early medical attention if symptoms persist or worsen over time.

It is important to note that while hemolytic anemia can be managed with proper treatment, it may not be curable in all cases, and ongoing monitoring and care are necessary to prevent complications and improve quality of life.

Pallor is often used as an indicator of underlying disease, particularly in conditions where there is a decrease in the amount of hemoglobin in the blood, such as anemia or blood loss. It can also be a sign of other diseases such as liver cirrhosis, kidney failure, and some types of cancer.

There are different types of pallor, including:

1. Anemic pallor: This is the most common type of pallor and is caused by a decrease in the number of red blood cells or hemoglobin in the blood. It can be seen in conditions such as iron deficiency anemia, vitamin deficiency anemia, and sickle cell anemia.
2. Post-inflammatory pallor: This type of pallor is caused by inflammation that leads to a decrease in blood flow to the skin. It can be seen in conditions such as erythema migrans (Lyme disease), and other inflammatory conditions.
3. Cirrhotic pallor: This type of pallor is caused by liver cirrhosis and is characterized by a pale, washed-out appearance of the skin.
4. Renal pallor: This type of pallor is caused by kidney failure and is characterized by a pale, washed-out appearance of the skin.
5. Cancer pallor: This type of pallor is caused by certain types of cancer, such as carcinomas and lymphomas, and is characterized by a pale, washed-out appearance of the skin.

In summary, pallor is a term used to describe an abnormal paleness or whiteness of the skin that can be caused by a variety of underlying medical conditions. It is often used as an indicator of illness and can be seen in a wide range of conditions, including anemia, inflammation, liver cirrhosis, kidney failure, and certain types of cancer.

A condition in which the kidneys gradually lose their function over time, leading to the accumulation of waste products in the body. Also known as chronic kidney disease (CKD).

Prevalence:

Chronic kidney failure affects approximately 20 million people worldwide and is a major public health concern. In the United States, it is estimated that 1 in 5 adults has CKD, with African Americans being disproportionately affected.

Causes:

The causes of chronic kidney failure are numerous and include:

1. Diabetes: High blood sugar levels can damage the kidneys over time.
2. Hypertension: Uncontrolled high blood pressure can cause damage to the blood vessels in the kidneys.
3. Glomerulonephritis: An inflammation of the glomeruli, the tiny blood vessels in the kidneys that filter waste and excess fluids from the blood.
4. Interstitial nephritis: Inflammation of the tissue between the kidney tubules.
5. Pyelonephritis: Infection of the kidneys, usually caused by bacteria or viruses.
6. Polycystic kidney disease: A genetic disorder that causes cysts to grow on the kidneys.
7. Obesity: Excess weight can increase blood pressure and strain on the kidneys.
8. Family history: A family history of kidney disease increases the risk of developing chronic kidney failure.

Symptoms:

Early stages of chronic kidney failure may not cause any symptoms, but as the disease progresses, symptoms can include:

1. Fatigue: Feeling tired or weak.
2. Swelling: In the legs, ankles, and feet.
3. Nausea and vomiting: Due to the buildup of waste products in the body.
4. Poor appetite: Loss of interest in food.
5. Difficulty concentrating: Cognitive impairment due to the buildup of waste products in the brain.
6. Shortness of breath: Due to fluid buildup in the lungs.
7. Pain: In the back, flank, or abdomen.
8. Urination changes: Decreased urine production, dark-colored urine, or blood in the urine.
9. Heart problems: Chronic kidney failure can increase the risk of heart disease and heart attack.

Diagnosis:

Chronic kidney failure is typically diagnosed based on a combination of physical examination findings, medical history, laboratory tests, and imaging studies. Laboratory tests may include:

1. Blood urea nitrogen (BUN) and creatinine: Waste products in the blood that increase with decreased kidney function.
2. Electrolyte levels: Imbalances in electrolytes such as sodium, potassium, and phosphorus can indicate kidney dysfunction.
3. Kidney function tests: Measurement of glomerular filtration rate (GFR) to determine the level of kidney function.
4. Urinalysis: Examination of urine for protein, blood, or white blood cells.

Imaging studies may include:

1. Ultrasound: To assess the size and shape of the kidneys, detect any blockages, and identify any other abnormalities.
2. Computed tomography (CT) scan: To provide detailed images of the kidneys and detect any obstructions or abscesses.
3. Magnetic resonance imaging (MRI): To evaluate the kidneys and detect any damage or scarring.

Treatment:

Treatment for chronic kidney failure depends on the underlying cause and the severity of the disease. The goals of treatment are to slow progression of the disease, manage symptoms, and improve quality of life. Treatment may include:

1. Medications: To control high blood pressure, lower cholesterol levels, reduce proteinuria, and manage anemia.
2. Diet: A healthy diet that limits protein intake, controls salt and water intake, and emphasizes low-fat dairy products, fruits, and vegetables.
3. Fluid management: Monitoring and control of fluid intake to prevent fluid buildup in the body.
4. Dialysis: A machine that filters waste products from the blood when the kidneys are no longer able to do so.
5. Transplantation: A kidney transplant may be considered for some patients with advanced chronic kidney failure.

Complications:

Chronic kidney failure can lead to several complications, including:

1. Heart disease: High blood pressure and anemia can increase the risk of heart disease.
2. Anemia: A decrease in red blood cells can cause fatigue, weakness, and shortness of breath.
3. Bone disease: A disorder that can lead to bone pain, weakness, and an increased risk of fractures.
4. Electrolyte imbalance: Imbalances of electrolytes such as potassium, phosphorus, and sodium can cause muscle weakness, heart arrhythmias, and other complications.
5. Infections: A decrease in immune function can increase the risk of infections.
6. Nutritional deficiencies: Poor appetite, nausea, and vomiting can lead to malnutrition and nutrient deficiencies.
7. Cardiovascular disease: High blood pressure, anemia, and other complications can increase the risk of cardiovascular disease.
8. Pain: Chronic kidney failure can cause pain, particularly in the back, flank, and abdomen.
9. Sleep disorders: Insomnia, sleep apnea, and restless leg syndrome are common complications.
10. Depression and anxiety: The emotional burden of chronic kidney failure can lead to depression and anxiety.

Symptoms of type 1 diabetes can include increased thirst and urination, blurred vision, fatigue, weight loss, and skin infections. If left untreated, type 1 diabetes can lead to serious complications such as kidney damage, nerve damage, and blindness.

Type 1 diabetes is diagnosed through a combination of physical examination, medical history, and laboratory tests such as blood glucose measurements and autoantibody tests. Treatment typically involves insulin therapy, which can be administered via injections or an insulin pump, as well as regular monitoring of blood glucose levels and appropriate lifestyle modifications such as a healthy diet and regular exercise.

Erythroleukemia typically affects adults in their 50s and 60s, although it can occur at any age. Symptoms may include fever, night sweats, weight loss, and fatigue. The cancer cells can spread to other parts of the body, including the spleen, liver, and lymph nodes.

Erythroleukemia is diagnosed through a combination of physical examination, blood tests, and bone marrow biopsy. Treatment typically involves chemotherapy and/or radiation therapy to kill cancer cells and restore normal blood cell production. In some cases, a bone marrow transplant may be necessary. The prognosis for erythroleukemia is generally poor, with a five-year survival rate of about 20%.

Erythroleukemia is classified as an acute leukemia, meaning it progresses rapidly and can lead to life-threatening complications if left untreated. It is important for patients to receive prompt and appropriate treatment to improve their chances of survival and quality of life.

Prevalence: Anemia, hemolytic, congenital is a rare disorder, affecting approximately 1 in 100,000 to 1 in 200,000 births.

Causes: The condition is caused by mutations in genes that code for proteins involved in hemoglobin synthesis or red blood cell membrane structure. These mutations can lead to abnormal hemoglobin formation, red blood cell membrane instability, and increased susceptibility to oxidative stress, which can result in hemolytic anemia.

Symptoms: Symptoms of anemia, hemolytic, congenital may include jaundice (yellowing of the skin and eyes), fatigue, weakness, pale skin, and shortness of breath. In severe cases, the condition can lead to life-threatening complications such as anemia, infections, and kidney failure.

Diagnosis: Anemia, hemolytic, congenital is typically diagnosed through a combination of physical examination, medical history, and laboratory tests, including blood smear examination, hemoglobin electrophoresis, and mutation analysis.

Treatment: Treatment for anemia, hemolytic, congenital depends on the specific underlying genetic cause and may include blood transfusions, folic acid supplements, antibiotics, and/or surgery to remove the spleen. In some cases, bone marrow transplantation may be necessary.

Prognosis: The prognosis for anemia, hemolytic, congenital varies depending on the specific underlying genetic cause and the severity of the condition. With appropriate treatment, many individuals with this condition can lead relatively normal lives, but in severe cases, the condition can be life-threatening.

There are several possible causes of methemoglobinemia, including:

1. Exposure to certain medications or chemicals, such as nitrates or aniline dyes.
2. Genetic disorders that affect the production or function of hemoglobin.
3. Infections, such as bacterial infections of the blood or respiratory tract.
4. Poor nutrition or malnutrition.
5. Certain chronic medical conditions, such as sickle cell anemia or thalassemia.

Methemoglobinemia can be diagnosed through a variety of tests, including:

1. Complete blood count (CBC) to measure the levels of methemoglobin in the blood.
2. Blood gas analysis to measure the partial pressure of oxygen and carbon dioxide in the blood.
3. Co-oximetry to measure the levels of methemoglobin and other forms of hemoglobin.
4. Urine tests to check for the presence of abnormal hemoglobin.
5. Genetic testing to identify inherited disorders that may be causing the condition.

Treatment of methemoglobinemia depends on the underlying cause and may include:

1. Administration of oxygen therapy to increase the amount of oxygen in the blood.
2. Use of medications to reduce the levels of methemoglobin and increase the levels of normal hemoglobin.
3. Transfusions of red blood cells to replace abnormal hemoglobin with normal hemoglobin.
4. Management of underlying medical conditions, such as infections or genetic disorders.
5. Dietary changes to address any nutritional deficiencies that may be contributing to the condition.

In severe cases of methemoglobinemia, hospitalization may be necessary to provide oxygen therapy and other treatments. In some cases, patients with methemoglobinemia may require long-term management and follow-up care to prevent complications and manage the underlying cause of the condition.

Excessive glucose in one's blood can attach to hemoglobin and raise the level of hemoglobin A1c. Hemoglobin and hemoglobin-like ... Hemoglobin Portland II (ζ2β2). In the fetus: Hemoglobin F (α2γ2) (PDB: 1FDH​). After birth: Hemoglobin A (adult hemoglobin) ( ... There is more than one hemoglobin gene: in humans, hemoglobin A (the main form of hemoglobin present in adults) is coded for by ... Variant forms that cause disease: Hemoglobin D-Punjab - (α2βD2) - A variant form of hemoglobin. Hemoglobin H (β4) - A variant ...
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 ...
Hemoglobin A1c was first separated from other forms of hemoglobin by Huisman and Meyering in 1958 using a chromatographic ... Glycated hemoglobin (glycohemoglobin, hemoglobin A1c, HbA1c, less commonly HbA1c, HgbA1c, Hb1c, etc., also A1C informally with ... Glycated hemoglobin is preferred over glycosylated hemoglobin to reflect the correct (non-enzymatic) process. Early literature ... Hemoglobin molecules clump together via cross-linking reactions, and these hemoglobin clumps (multimers) promote cell damage ...
... 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 mutant forms of hemoglobin in a population, caused by variations in genetics. Some well-known ...
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 ( ... v t e (Articles needing additional references from June 2020, All articles needing additional references, Hemoglobins, All stub ...
... 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 US National Library of Medicine Medical Subject Headings (MeSH) Hemoglobin A2 - The clinical significance ... 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 Hemoglobin, 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 ...
... is a type of alpha thalassemia caused by impaired production of three of the four alpha globins, coded by ... Hemoglobin Barts "Pathophysiology of alpha thalassemia". www.uptodate.com. Retrieved 2016-08-30. v t e (Articles with short ...
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 ...
The glycosylated hemoglobin test shows what a persons average blood glucose level was for the 2 to 3 months before the test. ... Glycosylated Hemoglobin Test (Hemoglobin A1c). Hemoglobin is the substance inside red blood cells that carries oxygen to the ... Glucose (a type of sugar) molecules in the blood normally become stuck to hemoglobin molecules - this means the hemoglobin has ... A blood test can measure the amount of glycosylated hemoglobin in the blood. The glycosylated hemoglobin test shows what a ...
Hemoglobin tests are usually conducted to test the blood for the amount of hemoglobin present in the blood. This blood test can ... What a Hemoglobin Test Detects. Hemoglobin testing can reveal numerous aspects of the blood. Anemia can occur if the bodys ... Why is a Hemoglobin Test Used?. Hemoglobin tests are done for three main reasons. One reason a test may be done to measure ... This test measures the bodys blood levels of hemoglobin. Hemoglobin is needed in the body to carry oxygen through out the body ...
Spectrophotometry of hemoglobin and hemoglobin derivatives. Download Prime PubMed App to iPhone, iPad, or Android ... "Spectrophotometry of Hemoglobin and Hemoglobin Derivatives." Advances in Clinical Chemistry, vol. 23, 1983, pp. 199-257. ... Spectrophotometry of Hemoglobin and Hemoglobin Derivatives. Adv Clin Chem. 1983;23:199-257. PubMed PMID: 6398614. ... Spectrophotometry of hemoglobin and hemoglobin derivatives.. Adv Clin Chem. 1983; 23:199-257.AC ...
What Is a Hemoglobin A1c Test?. A hemoglobin A1c test measures how much a persons glucose levels have been in and out of the ... Why Are Hemoglobin A1c Tests Done?. Doctors check hemoglobin A1c tests in kids with diabetes. The test helps them see how well ... A high hemoglobin A1c level may mean that a childs medicines need to be adjusted. Sometimes a hemoglobin A1c test is done as ... If too much glucose builds up in blood, it binds to hemoglobin. High hemoglobin A1c levels can happen when someones blood ...
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 ...
... is as effective as thrice-weekly dosing in improving hemoglobin (Hb) levels in HIV-positive patients who are anemic, Howard A. ... At week 8, hemoglobin had risen to 13.1 g/dL and 13.8 g/dL in the two groups. At week 16, hemoglobin was 12.9 g/dL and 13.5 g/ ... The change in hemoglobin was 2.5 g/dL over baseline in the thrice-weekly group of 76 evaluable patients and 2.8 g/dL in the ... Weekly Epoetin Ups Hemoglobin Levels, QOL in Anemic Patients. Feb 1, 2002. Oncology NEWS InternationalOncology NEWS ...
According to your letter, the subject product, Hemoglobin Powder, consists of hemoglobin collected from fresh pork blood, from ... RE: The tariff classification of Hemoglobin Powder from Germany. Dear Mr. Reynolds:. In your letter dated April 30, 2004, on ... After collection, the hemoglobin is spray dried at a low temperature, in accordance with the EU regulation for animal proteins ... The product specification sheet you submitted indicates that the hemoglobin powder is used, among other things, as an ...
... and seven used hematocrit rather than hemoglobin assessment. Of the 328 providers, 239 (73%) reported performing hemoglobin ... Methods of hemoglobin screening were classified as waived or nonwaived based on CLIA standards. A waived test is one that is a ... For a hemoglobin screening method to be determined accurate through proficiency testing, 80% of the tested specimens must be ... Questionnaires were mailed to each of the 418 CHDP providers that submitted hemoglobin data for greater than or equal to 100 ...
Awareness of hemoglobin level variability in dialysis patients is increasing, ... Variability in hemoglobin levels over time is very common, with almost 90% of patients experiencing hemoglobin level changes ... For example, 2-F represents 2 mo with hemoglobin ,11 g/dl during the first 3 mo; 4-F-S represents 4 mo with hemoglobin ,11 ... Defining Hemoglobin Variability. Hemoglobin variability was defined by two systems. By the first classification system, monthly ...
Kruatruchue, M; Bhaibulaya, M; Klingkamnaunkarn, K; Harinasuta, C; World Health Organization (‎World Health OrganizationWorld Health Organization, 1968)‎ ...
b,My wifes haemoglobin count is 9 %. Is this going to affect my wife in conceiving,/b,? Please explain me in simple words ... My wifes haemoglobin count is 9 %. Is this going to affect my wife in conceiving? Please explain me in simple words which is ... A:Anaemia is inadequate level of haemoglobin appropriate for age & sex. The most common cause of anaemia in pregnancy is ... Home » Frequently asked Questions on Health » Does low haemoglobin affect the chances of conception? ...
The 146 amino acid residues of the γ chain of human fetal hemoglobin have been placed in sequence. The fetal hemoglobin for ... The differences between the γ chains of human fetal hemoglobin and the β chains of human adult hemoglobin are responsible for ... The Amino Acid Sequence of the γ Chain of Human Fetal Hemoglobin W. A. Schroeder, J. Roger Shelton, Joan Balog Shelton, Jean ... The Amino Acid Sequence of the γ Chain of Human Fetal Hemoglobin ...
Hemoglobin C is an abnormal type of hemoglobin, the protein in red blood cells that carries oxygen. It is a type of ... Hemoglobin C disease is a blood disorder passed down through families. It leads to a type of anemia, which occurs when red ... Hemoglobin and hemoglobinopathies. In: Rifai N, Chiu RWK, Young I, Burnham CAD, Wittwer CT, eds. Tietz Textbook of Laboratory ... You are more likely to have hemoglobin C disease if someone in your family has had it. ...
Clinical webinar features an international panel of experts, including Dr. Lorenzo Berra, Anesthesiologist and ICU Medical Director at Massachusetts General Hospital, Dr. Beverley Hunt, Professor of Thrombosis and Haemostatis at Kings College London, and Dr. Mark Robinson, Consultant Haemotologist at Cambridge University.
High prevalence of haemoglobin S in the closed Egyptian community of Siwa Oasis ... High prevalence of haemoglobin S in the closed Egyptian community of Siwa Oasis ...
Title:Importance of many body effects in the kernel of hemoglobin for ligand binding. Authors:Cedric Weber, David D. ORegan, ... Download a PDF of the paper titled Importance of many body effects in the kernel of hemoglobin for ligand binding, by Cedric ... Download a PDF of the paper titled Importance of many body effects in the kernel of hemoglobin for ligand binding, by Cedric ... the kernel of the hemoglobin metalloprotein central to human respiration. We find that variations in Hunds exchange coupling ...
Hemoglobin-based oxygen carriers. Structural alterations that affect free radical formation ... Hemoglobin-based oxygen carriers. Structural alterations that affect free radical formation Journal Article (Journal Article) ... Hemoglobin-based oxygen carriers (HBOCs) are candidates for use as blood substitutes and resuscitation fluids. We determined ... Exposure to H2O2 also caused spectral changes (indicative of oxidative modifications of hemoglobin) at varied rates for the ...
Oxygen binding to haemoglobin is a reversible reaction. At lungs oxygen binds to haemoglobin to form the oxygen-haemoglobin ... C. Deoxyhaemoglobin (haemoglobin with no bound oxygen) *1. Prepare a diluted sample of haemoglobin. ... Haemoglobin Binding. *** Advanced Project Notice *** The following project is an ADVANCED project and may require handling of ... 1. Get a diluted sample of haemoglobin solution.. *2. Bubble CO gas through the sample. *i. CO is found in vehicle emission. ...
Plasmodium parasites on erythrocytes utilize hemoglobin as a source of amino acid. Uptake and transport of hemoglobin by ... In the result, ETRAMP10.3 was found to be localized to the PVM, cytostorm and hemoglobin transport vesicles, and to be an ... Analysis of parasitophorous vacuole membrane protein in hemoglobin transport and metabolism of malarial parasites. Research ... Presentation] Morphological observation of parasitophorous vacuole membrane during hemoglobin uptake of Plasmodium gametocyte ...
Inhibition of haemoglobin-mediated lipid oxidation in washed cod muscle and cod protein isolates by Fucus vesiculosus extract ... The effects of Fucus vesiculosus extract and fractions towards haemoglobin- (Hb-) catalysed lipid oxidation in washed cod ...
No 7629) dissolved in the AHD reagent corresponding to 30 g/L, 60 g/L, 90 g/L, 120 g/L,150 g/L and 180 g/L haemoglobin (final ... The conversion of haemoglobin to HiCN is not completed after a reasonable period of time. The presence of NaCl at physiological ... In the haemoglobin azide method measurement is made at 570 nm [8]. However, in some countries importation of azide is also ... The correlation of haemoglobin concentrations, which were read from calibration curves, were as good as the results for the ...
Allow specimen to clot completely at room temperature. Centrifuges separate serum from cells within 2 hours or collection and send 2.0 mL serum in a screw capped plastic vial ...
High HemoglobinHigh Hemoglobin, High Hemoglobin Levels High Hemoglobin Meaning: The problem of low blood is called anemia, but ... High Hemoglobin Levels - Meaning, Causes. admin. September 15, 2021. September 15, 2021. ...
The rate of data capture for haemoglobin A1 was 75.7%, and the mean level for study samples was 10.5% at one laboratory and ... Main outcome measures: Last glycated haemoglobin level measured in subjects for 1992 and published data from other studies ... samples of glycated haemoglobin had been processed at two laboratories with different methodologies and reference ranges. ... 10.0% at the other (similar values to those of comparable studies). These mean levels of haemoglobin A1 in representative ...
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HbA1c (Glycated haemoglobin) is made when glucose (sugar) in your body sticks to your red blood cells. When your body cant use ...
HPLC , ClinRep® & Tox® Kits , Alcoholism, Drug Abuse , Biogene Amines , Diabetes, Hemoglobin , Metabolic Diseases , Oxidative ... Diabetes, Hemoglobin , Metabolic Diseases , Oxidative Stress , Vitamin Status , Antiarrhythmics , Antiasthmatics , ... ClinRep® Complete Kit for Hemoglobin Variants and ß-Thalassemia Screening in Whole Blood for 500 assays, 1 pcs. ...
The HemoPoint® H2 Hemoglobin Analyzer provides a precise hemoglobin and hematocrit* measurement in just 30 seconds - One test. ... The HemoPoint® H2 Hemoglobin Analyzer provides a hemoglobin measurement and a hematocrit calculation* in about 30 seconds. ... Hematocrit result is calculated when hemoglobin result is within 12-18 g/dL. HemoPoint H2 Analyzer Brochure. HemoPoint-H2- ... HemoPoint H2 Hemoglobin Analyzer is CLIA waived and enables users to perform tests quickly and easily.. The innovative soft ...
... no one dares to lower your hemoglobin A1C naturally ask We have been like lower your hemoglobin A1C naturally this for the past ... Lower Your Hemoglobin A1C Naturally ?. Unless there is a slut who takes the initiative to come over and let me bully, otherwise ... The lower your hemoglobin A1C naturally only thing that made Hu Liang feel relieved was that although Li Qingyun was a little ... surrounded by a black armor, Lu Yu also showed a proud smile on his face! You must know that the thing lower your hemoglobin ...
  • Hemoglobinopathies are a group of common, inherited disorders of hemoglobin (Hb), resulting in the synthesis of structurally abnormal globin subunits. (arupconsult.com)
  • The hemoglobin evaluation reflexive cascade initially tests for abnormal hemoglobin. (arupconsult.com)
  • Hemoglobin C is an abnormal type of hemoglobin, the protein in red blood cells that carries oxygen. (adam.com)
  • Hemoglobin electrophoresis is abnormal in HbM disease, but normal with NADH-methemoglobin reductase deficiency [McKenzie 2010]. (cdc.gov)
  • Abnormal haemoglobin. (who.int)
  • In 1995, in conjunction with an assessment of county-specific variations in prevalence rates of anemia, the California Department of Health Services conducted a mail survey of CHDP providers to assess compliance with CLIA regulations for hemoglobin screening. (cdc.gov)
  • Anemia can occur if the body's hemoglobin levels are too low. (brighthub.com)
  • In the early 1990s, anemia correction was viewed simply as treatment with EPO along with correction of iron deficiency to increase hemoglobin levels from below 10 g/dl to within the initial label target range of 10 to 11 g/dl. (lww.com)
  • As experience with anemia correction grew and the potential side effects, including seizures and hypertension, occurred less frequently than anticipated from the initial trials, the United States Food and Drug Administration increased the target hemoglobin range to 10 to 12 g/dl. (lww.com)
  • High Hemoglobin Meaning: The problem of low blood is called anemia, but the excessive amount of blood in the body is also a disease, which is named polycythemia. (hemolevel.com)
  • Non-invasive hemoglobin estimation for preoperative anemia screening. (bvsalud.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)
  • of these, 16 providers were excluded from analysis because nine used a contracted commercial laboratory to perform their hemoglobin measurements, and seven used hematocrit rather than hemoglobin assessment. (cdc.gov)
  • Conclusions: Number of months with hemoglobin values below the target range, rather than hemoglobin variability itself, may be the primary driver of increased risk of death. (lww.com)
  • This study evaluated the association of packed red blood cell (PRBC) transfusion with mortality outcomes across hemoglobin levels amongst emergency center (EC) patients presenting with medical pathology in Kigali, Rwanda . (bvsalud.org)
  • As a person's blood sugar becomes higher, more of the person's hemoglobin becomes glycosylated. (kidshealth.org)
  • The glycosylated hemoglobin test shows what a person's average blood glucose level was for the 2 to 3 months before the test. (kidshealth.org)
  • A hemoglobin A1c test measures how much a person's glucose levels have been in and out of the healthy (or target) range during the last 2-3 months. (akronchildrens.org)
  • Standard Pulse-oximetry measurement of the oxygen saturation of hemoglobin does not provide accurate results in the presence of methemoglobinemia [Ralston et al. (cdc.gov)
  • A pulse oximeter is a device that measures the oxygen saturation of haemoglobin in arterial blood described as SPO2. (who.int)
  • The Masimo Pronto Pulse CO-Oximeter was utilized to estimate blood hemoglobin concentrations (SpHb), which were then compared with hemoglobin concentrations obtained via complete blood count . (bvsalud.org)
  • SpHb generally overestimated hemoglobin with a mean (± 1.96 × standard deviation) difference of 0.8 (-2.2, 3.9) g/dL. (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)
  • Free serum hemoglobin and haptoglobin levels are drawn to assess for hemolytic anemias. (cdc.gov)
  • The fetal hemoglobin for this investigation was isolated chromatographically from umbilical cord blood. (caltech.edu)
  • 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)
  • Maternal hemoglobin concentration at delivery, umbilical cord hemoglobin and ferritin were collected. (bvsalud.org)
  • The dependent and explanatory variables include ([hemoglobin at three months - umbilical cord hemoglobin / umbilical cord hemoglobin]*100) and immediate/delayed cord clamping, respectively. (bvsalud.org)
  • We support this model using linear-scaling first-principles calculations, in combination with dynamical mean-field theory, applied to heme, the kernel of the hemoglobin metalloprotein central to human respiration. (arxiv.org)
  • Hemoglobin is the iron-containing oxygen-transport metalloprotein in the red blood cells of vertebrates, and the tissues of some invertebrates. (sciencefairadventure.com)
  • Glucose (a type of sugar) molecules in the blood normally become stuck to hemoglobin molecules - this means the hemoglobin has become glycosylated (also referred to as hemoglobin A1c, or HbA1c). (kidshealth.org)
  • HbA1c (Glycated haemoglobin) is made when glucose (sugar) in your body sticks to your red blood cells. (letsgetchecked.com)
  • By plotting a graph, absorbance vs. wave length we can identify haemoglobin (no bound ligand), oxyhaemoglobin and carboxyhaemoglobin. (sciencefairadventure.com)
  • Patients â ¥15 years of age, treated for medical emergencies during 2013-16, with EC hemoglobin measurements were included. (bvsalud.org)
  • When the hemoglobin levels in the blood are elevated, polycythemia vera can occur. (brighthub.com)
  • Assessment of hemoglobin concentrations may facilitate optimization prior to surgery . (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)
  • Hemoglobin and hemoglobinopathies. (adam.com)
  • If too much glucose builds up in blood, it binds to hemoglobin. (akronchildrens.org)
  • At lungs oxygen binds to haemoglobin to form the oxygen-haemoglobin complex called oxyhaemoglobin. (sciencefairadventure.com)
  • But carbon monoxide binds to haemoglobin irreversibly and 200 times faster than oxygen to form a very bright red compound called carboxyhaemoglobin, meaning that small amounts of CO dramatically reduce hemoglobin's ability to transport oxygen. (sciencefairadventure.com)
  • In this retrospective, national study of associations between the degree of hemoglobin level variability in the first 6 mo of 2004 and subsequent mortality rates in the following 6 mo, 159,720 hemodialysis patients receiving epoetin therapy were studied. (lww.com)
  • The relationship between EC PRBC transfusion and patient mortality was evaluated using logistic regression , with stratified analyses performed at hemoglobin levels of 7 mg/dL and 5 mg/dL. (bvsalud.org)
  • This report summarizes the results of that survey, which indicate that, in California, many CHDP providers do not comply with CLIA-mandated quality-assurance practices for hemoglobin screening in their clinical laboratories. (cdc.gov)
  • The questionnaires assessed the type of health-care practice, the method used for hemoglobin screening, and quality-assurance practices. (cdc.gov)
  • Methods of hemoglobin screening were classified as waived or nonwaived based on CLIA standards. (cdc.gov)
  • Rates of compliance with CLIA regulations varied by type of health-care practice and hemoglobin screening method. (cdc.gov)
  • The effects of Fucus vesiculosus extract and fractions towards haemoglobin- (Hb-) catalysed lipid oxidation in washed cod muscle system and cod protein isolates during ice storage were examined. (matis.is)
  • The glucose remains attached to the hemoglobin for the life of the red blood cell, or about 2 to 3 months. (kidshealth.org)
  • Hemoglobin A1c (HbA 1c ) levels should be measured every 3 months and treatment adjusted if goals for both HbA 1c and blood glucose are not met. (medscape.com)
  • In 1967, the International Council for Standardization in Haematology (ICSH) recommended the haemoglobin cyanide (HiCN) method as the reference method for use [1]. (who.int)
  • In 1985 WHO established the second haemoglobin cyanide reference material [5] and recommended the HiCN method be given the status of an international reference procedure. (who.int)
  • In heavy smokers, up to 20% of the oxygen-active sites can be blocked by CO. In similar fashion, hemoglobin also has competitive binding affinity for cyanide (CN-), sulfur monoxide(SO), nitrogen dioxide (NO2), and sulfide(S2-), including hydrogen sulfide (H2S). (sciencefairadventure.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 high hemoglobin A1c level may mean that a child's medicines need to be adjusted. (akronchildrens.org)
  • In this open-label study, HIV-positive patients with a hemoglobin level of 12 g/dL or less were randomized to receive 100 U/kg of epoetin three times a week or 40,000 U once a week for 16 weeks. (cancernetwork.com)
  • Background/objectives: Awareness of hemoglobin level variability in dialysis patients is increasing, as is interest in its potential implications. (lww.com)
  • Anaemia is inadequate level of haemoglobin appropriate for age & sex. (ndtv.com)
  • Simple analytical instruments for haemoglobin measurement using the HiCN method, appropriate at the primary level, are not available. (who.int)
  • Reports from Africa reveal that haemoglobin measurement has the poorest precision and reproducibility among all common laboratory indicators [6]. (who.int)
  • CHICAGO-Once-a-week dosing of recombinant human erythropoietin (epoetin alfa, Epogen, Procrit) is as effective as thrice-weekly dosing in improving hemoglobin (Hb) levels in HIV-positive patients who are anemic, Howard A. Grossman, MD, said at the Interscience Conference on Antimicrobial Agents and Chemotherapy (ICAAC abstract 254). (cancernetwork.com)
  • Findings from an interim analysis of 156 patients indicate that HIV-positive individuals receiving epoetin once a week achieve the same degree of improvement in hemoglobin levels and quality of life assessments as those who take the medication three times weekly. (cancernetwork.com)
  • The delayed cord clamping benefits the hemoglobin status of infants, especially those born to non anemic mothers. (bvsalud.org)
  • Monitoring the bloods hemoglobin levels can help test for many medical disorders. (brighthub.com)
  • During a meeting in Geneva on September 2002, the World Health Organization (WHO) Working Group on Anaemia noted that blood haemoglobin determination for diagnosing and monitoring treatment of anaemia in populations of countries with limited resources is still an unsolved problem. (who.int)
  • Results of search for 'su:{Hemoglobins. (who.int)
  • Hemoglobin testing can reveal numerous aspects of the blood. (brighthub.com)
  • After collection, the hemoglobin is spray dried at a low temperature, in accordance with the EU regulation for animal proteins, and put up packed in 25 kg bags. (faqs.org)
  • Blood samples from 15 spray painters applying HDI-containing paint were analyzed for hemoglobin HDA (HDA-Hb) and N-acetyl-1,6-hexamethylene diamine (monoacetyl-HDA-Hb) by GC-MS. HDA-Hb was detected in the majority of workers (≤1.2-37ng/g Hb), whereas monoacetyl-HDA-Hb was detected in one worker (0.06 ng/g Hb). (cdc.gov)
  • Contact your health care provider if you have symptoms of hemoglobin C disease. (adam.com)
  • Hemoglobin tests are done for three main reasons. (brighthub.com)
  • Why Are Hemoglobin A1c Tests Done? (akronchildrens.org)
  • 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)
  • According to your letter, the subject product, Hemoglobin Powder, consists of hemoglobin collected from fresh pork blood, from animals slaughtered at EU-approved slaughterhouses under veterinarian control. (faqs.org)
  • High hemoglobin A1c levels can happen when someone's blood sugars have been higher than their healthy range. (akronchildrens.org)
  • transiently and persistently high hemoglobin levels were not associated with increased risk of death. (lww.com)
  • ABSTRACT Accurate, economical methods for haemoglobin determination by laboratories in countries with limited resources are not available. (who.int)
  • The results indicate that the AHD575 method is suitable for measuring haemoglobin in laboratories at all levels. (who.int)
  • Despite its deficiencies, the use of the HiCN method improved haemoglobin measurement in laboratories using automated techniques. (who.int)
  • Testing hemoglobin levels can also be used to view a persons overall health. (brighthub.com)
  • Hemoglobin is the substance inside red blood cells that carries oxygen to the cells of the body. (kidshealth.org)
  • Hemoglobin is needed in the body to carry oxygen through out the body. (brighthub.com)
  • 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 hemoglobin test measures how much hemoglobin is in your blood. (medlineplus.gov)
  • The hemoglobin test is a common test and is almost always done as part of a complete blood count (CBC). (medlineplus.gov)
  • A blood test can measure the amount of glycosylated hemoglobin in the blood. (kidshealth.org)
  • Hemoglobin test are often given to test for underlying health conditions. (brighthub.com)
  • This test measures the body's blood levels of hemoglobin. (brighthub.com)
  • Why is a Hemoglobin Test Used? (brighthub.com)
  • One reason a test may be done to measure hemoglobin levels is to monitor previous medical conditions. (brighthub.com)
  • In order to diagnose many medical conditions, a hemoglobin test is often conducted. (brighthub.com)
  • The test for measuring hemoglobin levels is relatively simple. (brighthub.com)
  • What Is a Hemoglobin A1c Test? (akronchildrens.org)
  • Sometimes a hemoglobin A1c test is done as part of a routine checkup to screen for problems. (akronchildrens.org)
  • If you have questions about the hemoglobin A1c test or what the test results mean, talk to your doctor. (akronchildrens.org)
  • Although not required under CLIA, 75 (31.4%) of these providers reported participation in a proficiency testing program for hemoglobin. (cdc.gov)
  • Questionnaires were mailed to each of the 418 CHDP providers that submitted hemoglobin data for greater than or equal to 100 children aged 6-59 months to the Pediatric Nutrition Surveillance System (PedNSS) during 1993. (cdc.gov)
  • The 146 amino acid residues of the γ chain of human fetal hemoglobin have been placed in sequence. (caltech.edu)
  • The differences between the γ chains of human fetal hemoglobin and the β chains of human adult hemoglobin are responsible for the differences in the properties of the two molecules. (caltech.edu)