Hemoglobins: 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.Hemoglobin A: Normal adult human hemoglobin. The globin moiety consists of two alpha and two beta chains.Hemoglobins, Abnormal: 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.Fetal Hemoglobin: 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.Hemoglobin, Sickle: 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.Hemoglobin C: 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.Oxyhemoglobins: 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.Hemoglobin A, Glycosylated: 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.Hemoglobin E: 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.Hemoglobin A2: 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.MethemoglobinTruncated Hemoglobins: 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.Anemia: A reduction in the number of circulating ERYTHROCYTES or in the quantity of HEMOGLOBIN.Hemoglobinopathies: A group of inherited disorders characterized by structural alterations within the hemoglobin molecule.CarboxyhemoglobinHemoglobinometry: Measurement of hemoglobin concentration in blood.Oxygen: 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.Hemoglobin C Disease: 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.Blood Substitutes: 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.Hemoglobin J: 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.Hemoglobin H: 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.Diphosphoglyceric AcidsAnemia, Sickle Cell: 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.Erythrocytes: Red blood cells. Mature erythrocytes are non-nucleated, biconcave disks containing HEMOGLOBIN whose function is to transport OXYGEN.2,3-Diphosphoglycerate: 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)Globins: A superfamily of proteins containing the globin fold which is composed of 6-8 alpha helices arranged in a characterstic HEME enclosing structure.Heme: The color-furnishing portion of hemoglobin. It is found free in tissues and as the prosthetic group in many hemeproteins.Thalassemia: 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.Iron: 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.Hematocrit: 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.Erythropoietin: 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.Hemoglobin SC Disease: 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: 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)Hematinics: 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.Erythrocyte Count: The number of RED BLOOD CELLS per unit volume in a sample of venous BLOOD.Erythrocyte Indices: 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, Iron-Deficiency: 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.Phytic Acid: Complexing agent for removal of traces of heavy metal ions. It acts also as a hypocalcemic agent.Haptoglobins: 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.Blood Protein Electrophoresis: Electrophoresis applied to BLOOD PROTEINS.beta-Thalassemia: 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.Sickle Cell Trait: The condition of being heterozygous for hemoglobin S.Hemoglobin M: 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.Antisickling Agents: Agents used to prevent or reverse the pathological events leading to sickling of erythrocytes in sickle cell conditions.alpha-Thalassemia: 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.Ferritins: 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.alpha-Globins: 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.Erythrocytes, Abnormal: Oxygen-carrying RED BLOOD CELLS in mammalian blood that are abnormal in structure or function.Myoglobin: A conjugated protein which is the oxygen-transporting pigment of muscle. It is made up of one globin polypeptide chain and one heme group.Hemolysis: The destruction of ERYTHROCYTES by many different causal agents such as antibodies, bacteria, chemicals, temperature, and changes in tonicity.beta-Globins: 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.Hydrogen-Ion Concentration: 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, Hypochromic: 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)Erythropoiesis: 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.Hemoglobinuria: 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.Polycythemia: An increase in the total red cell mass of the blood. (Dorland, 27th ed)Hemin: 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.Spectrophotometry: The art or process of comparing photometrically the relative intensities of the light in different parts of the spectrum.Electrophoresis, Cellulose Acetate: Electrophoresis in which cellulose acetate is the diffusion medium.Pregnancy Complications, Hematologic: 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.Heinz Bodies: 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.Exchange Transfusion, Whole Blood: 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.Hematologic Tests: Tests used in the analysis of the hemic system.Annelida: 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)Kinetics: The rate dynamics in chemical or physical systems.Reticulocyte Count: 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.Oligochaeta: A class of annelid worms with few setae per segment. It includes the earthworms such as Lumbricus and Eisenia.Hemeproteins: Proteins that contain an iron-porphyrin, or heme, prosthetic group resembling that of hemoglobin. (From Lehninger, Principles of Biochemistry, 1982, p480)Blood Glucose: Glucose in blood.Blood Transfusion: The introduction of whole blood or blood component directly into the blood stream. (Dorland, 27th ed)Iron Isotopes: 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.Diabetes Mellitus: A heterogeneous group of disorders characterized by HYPERGLYCEMIA and GLUCOSE INTOLERANCE.Spectroscopy, Near-Infrared: 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.Reticulocytes: 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.Diabetes Mellitus, Type 2: 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.Fructosamine: 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, Starch Gel: Electrophoresis in which a starch gel (a mixture of amylose and amylopectin) is used as the diffusion medium.Anemia, Hemolytic: A condition of inadequate circulating red blood cells (ANEMIA) or insufficient HEMOGLOBIN due to premature destruction of red blood cells (ERYTHROCYTES).Isoelectric Focusing: 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.Hemoglobin Subunits: The PROTEIN SUBUNITS that comprise multimeric HEMOGLOBINS.Photolysis: Chemical bond cleavage reactions resulting from absorption of radiant energy.Macromolecular Substances: 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.Blood Cell Count: 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.Protein Conformation: 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).Time Factors: Elements of limited time intervals, contributing to particular results or situations.Erythrocyte Transfusion: The transfer of erythrocytes from a donor to a recipient or reinfusion to the donor.Protein Binding: 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.Ferrous Compounds: Inorganic or organic compounds that contain divalent iron.Allosteric Regulation: 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.Renal Dialysis: Therapy for the insufficient cleansing of the BLOOD by the kidneys based on dialysis and including hemodialysis, PERITONEAL DIALYSIS, and HEMODIAFILTRATION.Chromatography, High Pressure Liquid: Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.Vitreoscilla: 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)Erythrocyte Volume: Volume of circulating ERYTHROCYTES . It is usually measured by RADIOISOTOPE DILUTION TECHNIQUE.Erythrocyte Aging: 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.Partial Pressure: 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)Polychaeta: A class of marine annelids including sandworms, tube worms, clamworms, and fire worms. It includes also the genus Myxicola infundibulum.Hemodilution: 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.Oxidation-Reduction: 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).Bivalvia: 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.Recombinant Proteins: Proteins prepared by recombinant DNA technology.Pallor: A clinical manifestation consisting of an unnatural paleness of the skin.Chironomidae: A family of nonbiting midges, in the order DIPTERA. Salivary glands of the genus Chironomus are used in studies of cellular genetics and biochemistry.gamma-Globins: 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.Oximetry: 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.Phenylhydrazines: Diazo derivatives of aniline, used as a reagent for sugars, ketones, and aldehydes. (Dorland, 28th ed)SulfhemoglobinKidney Failure, Chronic: 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.Nitric Oxide: 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.Hydroxyurea: An antineoplastic agent that inhibits DNA synthesis through the inhibition of ribonucleoside diphosphate reductase.Iron, Dietary: 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.Protoporphyrins: 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.Amino Acid Sequence: 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.Spectrum Analysis, Raman: Analysis of the intensity of Raman scattering of monochromatic light as a function of frequency of the scattered light.Blood Chemical Analysis: An examination of chemicals in the blood.Erythrocyte Membrane: The semi-permeable outer structure of a red blood cell. It is known as a red cell 'ghost' after HEMOLYSIS.Erythrocruorins: 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.Treatment Outcome: 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.Spectrum Analysis: 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)Mercuribenzoates: Mercury-containing benzoic acid derivatives.Prospective Studies: 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.Biological Markers: 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.Whales: 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.Chromatography, Ion Exchange: 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.Diabetes Mellitus, Type 1: 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.Histidine: An essential amino acid that is required for the production of HISTAMINE.Leghemoglobin: 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.Risk Factors: 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.Hypoglycemic Agents: Substances which lower blood glucose levels.Altitude: A vertical distance measured from a known level on the surface of a planet or other celestial body.Leukemia, Erythroblastic, Acute: A myeloproliferative disorder characterized by neoplastic proliferation of erythroblastic and myeloblastic elements with atypical erythroblasts and myeloblasts in the peripheral blood.Transferrin: 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.Anemia, Hemolytic, Congenital: Hemolytic anemia due to various intrinsic defects of the erythrocyte.Serum Albumin: A major protein in the BLOOD. It is important in maintaining the colloidal osmotic pressure and transporting large organic molecules.Molecular Sequence Data: 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.Retrospective Studies: 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.Osmotic Fragility: 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.Pregnancy: The status during which female mammals carry their developing young (EMBRYOS or FETUSES) in utero before birth, beginning from FERTILIZATION to BIRTH.Bloodletting: 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.Reference Values: 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.Erythroblasts: 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.Nutritional Status: State of the body in relation to the consumption and utilization of nutrients.Erythroid Precursor Cells: 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.Oxygen Consumption: 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)Chromium Isotopes: 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.Methemoglobinemia: 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)Amino Acids: 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.Dicrocoelium: 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.Blood Proteins: Proteins that are present in blood serum, including SERUM ALBUMIN; BLOOD COAGULATION FACTORS; and many other types of proteins.Binding Sites: The parts of a macromolecule that directly participate in its specific combination with another molecule.Erythrocyte Deformability: Ability of ERYTHROCYTES to change shape as they pass through narrow spaces, such as the microvasculature.
Coupling of the oxygen-linked interaction energy for inositol hexakisphosphate and bezafibrate binding to human HbA0. (1/606)
The energetics of signal propagation between different functional domains (i.e. the binding sites for O2, inositol hexakisphospate (IHP), and bezafibrate (BZF)) of human HbA0 was analyzed at different heme ligation states and through the use of a stable, partially heme ligated intermediate. Present data allow three main conclusions to be drawn, and namely: (i) IHP and BZF enhance each others binding as the oxygenation proceeds, the coupling free energy going from close to zero in the deoxy state to -3.4 kJ/mol in the oxygenated form; (ii) the simultaneous presence of IHP and BZF stabilizes the hemoglobin T quaternary structure at very low O2 pressures, but as oxygenation proceeds it does not impair the transition toward the R structure, which indeed occurs also under these conditions; (iii) under room air pressure (i.e. pO2 = 150 torr), IHP and BZF together induce the formation of an asymmetric dioxygenated hemoglobin tetramer, whose features appear reminiscent of those suggested for transition state species (i.e. T- and R-like tertiary conformation(s) within a quaternary R-like structure). (+info)Altered ligand rebinding kinetics due to distal-side effects in hemoglobin chico (Lysbeta66(E10) --> thr). (2/606)
Hb Chico is an unusual human hemoglobin variant that has lowered oxygen affinity, but unaltered cooperativity and anion sensitivity. Previous studies showed these features to be associated with distal-side heme pocket alterations that confer increased structural rigidity on the molecule and that increase water content in the beta-chain heme pocket. We report here that the extent of nanosecond geminate rebinding of oxygen to the variant and its isolated beta-chains is appreciably decreased. Structural alterations in this variant decrease its oxygen recombination rates without significantly altering rates of migration out of the heme pocket. Data analysis indicates that one or more barriers that impede rebinding of oxygen from docking sites in the heme pocket are increased, with less consequence for CO rebinding. Resonance Raman spectra show no significant alterations in spectral regions sensitive to interactions between the heme iron and the proximal histidine residue, confirming that the functional differences in the variant are due to distal-side heme pocket alterations. These effects are discussed in the context of a schematic representation of heme pocket wells and barriers that could aid the design of novel hemoglobins with altered ligand affinity without loss of the normal allosteric responses that facilitate unloading of oxygen to respiring tissues. (+info)Sickle hemoglobin polymer melting in high concentration phosphate buffer. (3/606)
Sickle cell hemoglobin (HbS) prepared in argon-saturated 1.8 M phosphate buffer was rapidly mixed with carbon monoxide (CO)-saturated buffer. The binding of CO to the sickle hemoglobin and the simultaneous melting of the hemoglobin polymers were monitored by transmission spectroscopy (optical absorption and turbidity). Changes in the absorption profile were interpreted as resulting from CO binding to deoxy-HbS while reduced scattering (turbidity) was attributed to melting (depolymerization) of the HbS polymer phase. Analysis of the data provides insight into the mechanism and kinetics of sickle hemoglobin polymer melting. Conversion of normal deoxygenated, adult hemoglobin (HbA) in high concentration phosphate buffer to the HbA-CO adduct was characterized by an average rate of 83 s-1. Under the same conditions, conversion of deoxy-HbS in the polymer phase to the HbS-CO adduct in the solution phase is characterized by an average rate of 5.8 s-1 via an intermediate species that grows in with a 36 s-1 rate. Spectral analysis of the intermediate species suggests that a significant amount of CO may bind to the polymer phase before the polymer melts. (+info)Physiological effects of modified hemoglobin as an oxygen-carrying macromolecule. (4/606)
A stabilized hemoglobin as oxygen-carrying macromolecules was developed. It had approximately 90,000 dalton molecular weights and its intravascular half life was 36 hours. Its molecular size was less than 0.1 micron. Its hemoglobin concentration was 6% and P50 value was 24 mmHg. The oxygen carried inside the plasma performs differently than the oxygen carried inside the red cells. Only less than 0.3 ml of oxygen in 100 ml of blood is available inside the plasma while 14-19 ml of oxygen is carried inside the red cells. Thus, less than 5 ml of oxygen is available inside the plasma of the entire body. When a patient develops hypovolemic shock, the red cells are bypassed and are not perfused directly inside the tissues. However, the plasma should reach such hypoxic tissues. Thus, infusion of oxygen-carrying macromolecules in the plasma should be therapeutically effective even if less than 100 ml of stabilized hemoglobin solution were infused under shock conditions. The basic physiology of oxygen-carrying macromolecules is described in detail, which is different from the oxygen carried inside the red cells. (+info)Metal complexes as allosteric effectors of human hemoglobin: an NMR study of the interaction of the gadolinium(III) bis(m-boroxyphenylamide)diethylenetriaminepentaacetic acid complex with human oxygenated and deoxygenated hemoglobin. (5/606)
The boronic functionalities on the outer surface of the Gd(III) bis(m-boroxyphenylamide)DTPA complex (Gd(III)L) enable it to bind to fructosamine residues of oxygenated glycated human adult hemoglobin. The formation of the macromolecular adduct can be assessed by NMR spectroscopy via observation of the enhancement of the solvent water proton relaxation rate. Unexpectedly, a strong binding interaction was also observed for the oxygenated unglycated human adult hemoglobin, eventually displaying a much higher relaxation enhancement. From relaxation rate measurements it was found that two Gd(III)L complexes interact with one hemoglobin tetramer (KD = 1.0 x 10(-5) M and 4.6 x 10(-4) M, respectively), whereas no interaction has been observed with monomeric hemoproteins. A markedly higher affinity of the Gd(III)L complex has been observed for oxygenated and aquo-met human adult hemoglobin derivatives with respect to the corresponding deoxy derivative. Upon binding, a net change in the quaternary structure of hemoglobin has been assessed by monitoring the changes in the high-resolution 1H-NMR spectrum of the protein as well as in the Soret absorption band. On the basis of these observations and the 11B NMR results obtained with the diamagnetic La(III)L complex, we suggest that the interaction between the lanthanide complex and deoxygenated, oxygenated, and aquo-met derivatives of human adult hemoglobin takes place at the 2, 3-diphosphoglycerate (DPG) binding site, through the formation of N-->B coordinative bonds at His143beta and His2beta residues of different beta-chains. The stronger binding to the oxygenated form is then responsible for a shift of the allosteric equilibrium toward the high-affinity R-state. Accordingly, Gd(III)L affinity for oxygenated human fetal hemoglobin (lacking His143beta) is significantly lower than that observed for the unglycated human adult tetramer. (+info)Fetal hemoglobin (HbF) synthesis in baboons, Papio cynocephalus. Analysis of fetal and adult hemoglobin synthesis during fetal development. (6/606)
Fetal hemoglobin (HbF) and adult hemoglobin (HbA) synthesis was studied in fetal baboons, Papio cynocephalus, to determine the normal pattern of hemoglobin production during fetal development. Fetuses ranging from 53 to 180 days gestation (term gestation 184 days) were used. Erythroid cells were incubated with 3H-L-leucine, and the rates of globin chain synthesis and the distribution of radioactivity into hemoglobin intermediates and completed hemoglobin molecules were determined. Gamma chain synthesis accounted for approximately 97% of the total nonalpha chain synthesis up to 140 days gestation; beta chain synthesis accounted for the remainder. After 140 days gestation, approximately equal quantities of gamma and beta chain were synthesized in the bone marrow. Prior to 140 days gestation, total alpha chain synthesis was 30% greater than total non-alpha chain synthesis, while there was balanced chain synthesis after 140 days gestation. During the period of excess alpha chain synthesis, fetal erythrocytes contained a large pool of alpha-hemoglobin (alpha chain with heme attached) molecules uncombined with beta or gamma chains. In view of the possibility that alpha chains may have a lower affinity for gamma chains than beta chains, excess alpha chain synthesis may be required to maintain low levels of free gamma chains. (+info)Kinetic studies on the binding affinity of human hemoglobin for the 4th carbon monoxide molecule, L4. (7/606)
L4, the affinity of hemoglobin for the 4th CO molecule, has been determined for human adult hemoglobin (HbA) as a function of pH and the presence of organic phosphates by measuring the kinetic parameters for the reaction. l'4, the rate of combination of CO with the triliganded molecule, was measured by flash photolysis while l4, the rate of CO dissociation for the ligand-saturated molecule, was measured by ligand replacement. L4 is pH-dependent and affected by 2,3-diphosphoglycerate. Additionally, this pH dependence of the high affinity state is largely eliminated by carboxypeptidase A digestion. L4 for human fetal hemoglobin (HbF) in phosphate buffers was also determined and found to be pH-dependent. These results cannot be reconciled within the framework of the two-state allosteric model. Additional structures in the conformational equilibrium due to either intermediates in the T to R transition or two or more R states must exist. (+info)Iron nutritional status in preterm infants fed formulas fortified with iron. (8/606)
AIMS: To prospectively evaluate the iron nutritional status of preterm infants fed either a term (0.5 mg/dl iron) or preterm (0.9 mg/dl) formulas fortified with iron after hospital discharge. METHODS: Healthy low birthweight preterm infants were randomly assigned into three groups at the time of hospital discharge. Group A were fed an iron fortified preterm formula (0.9 mg/dl iron) until 6 months corrected age; group B, a fortified term formula (0.5 mg/l iron) until 6 months corrected age group C, the preterm formula between hospital discharge and term, then the term formula until 6 months corrected age. RESULTS: Seventy eight infants were followed up to 6 months corrected age. Iron intake from formula differed significantly between the groups (A, 1.17 mg/kg/day (SD 0.32) > C, 0. 86 mg/kg/day (SD 0.40) = B, 0.81 mg/kg/day (SD 0.23); p < 0.0001). Haemoglobin concentrations were similar to those of iron sufficient preterm infants of the same postnatal age, and term infants of the same postmenstrual age (after 3 months of age). There were no significant differences in haemoglobin concentration (p = 0.391), plasma ferritin (A vs B, p = 0.322), or in the incidence of iron deficiency (A vs B, p = 0.534). CONCLUSIONS: Iron fortified formulas containing between 0.5 and 0.9 mg/dl iron seem to meet the iron nutritional needs of preterm infants after hospital discharge. (+info)
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MoleculeElectrophoresisMoleculesForms of hemoglobinLungsAnemiaFetal hemoglobinType of hemoglobinForm of hemoglobin2019Protein in red bloodVariantsTotal hemoglobinGlobinGlucoseTissuesThalassemiaStructure of hemoglobinTetramerSubunitsHbA1cAdult hemoglobinProteinsLevelsBindsDiabetesMeasure hemoglobinAmount of glycated hemoglobinPercentage of glycated hemoglobinHuman hemoglobinsDisordersGramsTypes of hemoglobinConcentrationMeasurementSickle Cell HemoglobinNitric oxideLevelGenesDeficiencyCarry oxygenGlycosylated hemoglobin in the bMeasuring the hemoglobin contentBindDissolved oxygen in bloodBiochemistryGeneTestConcentrationsSearchClaim 1 whereinDefinitionHigh-affinityCarbon dioxide
Molecule15
- The mammalian hemoglobin molecule can bind (carry) up to four oxygen molecules. (wikipedia.org)
- A hemoglobin molecule is composed of a protein group, known as globin, and four heme groups, each associated with an iron atom. (infoplease.com)
- Each hemoglobin molecule also has attached a single cysteine amino acid, which attracts nitric oxide from the lungs. (infoplease.com)
- Then the oxygen- and nitric oxide-free hemoglobin molecule picks up carbon dioxide and free nitric oxide and transports both back to the lungs, where they are exhaled as waste. (infoplease.com)
- Ninety percent of the protein in red blood cells is made up of hemoglobin, the main oxygen transport molecule in mammals. (dictionary.com)
- A protein with four iron-containing subunits called hemes, hemoglobin is a complex molecule with a complex function. (dictionary.com)
- When the last of the four heme subunits loses its oxygen, the structure of hemoglobin changes again, so that the size of the opening from the environment to the heme groups decreases, making it difficult for an oxygen molecule to rebind to the hemoglobin. (dictionary.com)
- Create healthcare diagrams like this example called Hemoglobin Molecule in minutes with SmartDraw. (smartdraw.com)
- Diagram of the shape of the hemoglobin molecule found in red blood cells that carries the oxygen. (smartdraw.com)
- The Information Center for Sickle Cell and Thalassemic Disorders explains that hemoglobin is a very important molecule which, like other proteins, is created from genetic codes in cellular DNA. (reference.com)
- Each haemoglobin molecule consists of four iron-containing parts ( haems ) and four protein chains ( globins ). (encyclopedia.com)
- Each haemoglobin molecule can combine with four oxygen molecules, but with no more. (encyclopedia.com)
- These conserved positions are especially important for the function of the hemoglobin molecule. (kenyon.edu)
- HBOCs use the natural oxygen-carrying molecule called hemoglobin (Hb) to carry oxygen throughout the body. (fda.gov)
- The hemoglobin molecule contains iron, an essential mineral found in our diet. (blood.ca)
Electrophoresis27
- What Is a Hemoglobin Electrophoresis Test? (kidshealth.org)
- A hemoglobin electrophoresis test measures the different types of hemoglobin in the blood. (kidshealth.org)
- Why Are Hemoglobin Electrophoresis Tests Done? (kidshealth.org)
- How Should We Prepare for a Hemoglobin Electrophoresis Test? (kidshealth.org)
- This can affect the hemoglobin electrophoresis test. (kidshealth.org)
- Can I Stay With My Child During a Hemoglobin Electrophoresis Test? (kidshealth.org)
- How Long Does a Hemoglobin Electrophoresis Test Take? (kidshealth.org)
- When Are Hemoglobin Electrophoresis Test Results Ready? (kidshealth.org)
- Are There Any Risks From Hemoglobin Electrophoresis Tests? (kidshealth.org)
- A hemoglobin electrophoresis test is a safe procedure with minimal risks. (kidshealth.org)
- If you have questions about the hemoglobin electrophoresis test, speak with your doctor or the health professional doing the blood draw. (kidshealth.org)
- The electrophoresis process takes advantage of the fact that hemoglobin types have different electrical charges. (kidshealth.org)
- During electrophoresis, an electrical current is passed through the hemoglobin in a blood sample, which causes the hemoglobin types to separate at different rates and form bands. (kidshealth.org)
- A doctor may order hemoglobin electrophoresis to help diagnose diseases (called hemoglobinopathies) involving abnormal hemoglobin production, such as sickle cell disease and thalassemia. (kidshealth.org)
- In many states, a hemoglobin electrophoresis is performed as part of a series of newborn screening blood tests, primarily so that kids with sickle cell anemia can be diagnosed, monitored, and treated early to prevent potentially life-threatening complications. (kidshealth.org)
- Hemoglobin electrophoresis is considered a safe procedure. (kidshealth.org)
- See all of hemoglobin electrophoresis , no other writeups in this node. (everything2.com)
- This technique is a type of electrophoresis used to separate hemoglobin proteins from each other with an electric current . (everything2.com)
- Hemoglobin electrophoresis is used as a screening test to identify normal and abnormal hemoglobins and assess their quantity. (medscape.com)
- Hemoglobin electrophoresis has been superseded by more rapid, sensitive, and quantitative methods of hemoglobin separation. (medscape.com)
- [ 3 ] Citrate agar electrophoresis at pH 6.0-6.2 provides better resolution for different hemoglobin variants. (medscape.com)
- Evaluation of a suspected hemoglobinopathy should include electrophoresis of a hemolysate to detect abnormal hemoglobins and quantification of HbA 2 and HbF with column chromatography. (medscape.com)
- A method useful for determining the content of a first hemoglobin in a blood sample which also contains other forms of hemoglobin is based on capillary electrophoresis. (google.com)
- A fetal hemoglobin test (Hgb electrophoresis) measures the level of fetal hemoglobin (Hemoglobin F or HbF) in the blood of infants and children. (encyclopedia.com)
- Fetal hemoglobin is one of six types of hemoglobin measured in the clinical laboratory by a method called hemoglobin electrophoresis. (encyclopedia.com)
- Abnormal types of hemoglobin include Hgb S and Hgb C. All types of hemoglobin are electrically charged, which enables them to be identified and quantified in the laboratory by hemoglobin electrophoresis techniques. (encyclopedia.com)
- The gel electrophoresis pattern for hemoglobin S shows which of the following migration patterns? (medialab.com)
Molecules11
- Haemoglobin and haemoglobin-like molecules are also found in many invertebrates, fungi, and plants. (wikipedia.org)
- Hemoglobin consists of protein subunits (the "globin" molecules), and these proteins, in turn, are folded chains of a large number of different amino acids called polypeptides . (wikipedia.org)
- Hemoglobin deficiency may be a result of structural abnormality in the hemoglobin molecules themselves. (infoplease.com)
- You can't fully understand how hemoglobin molecules interact until you've seen them depicted through a classical pas de deux. (dictionary.com)
- Each hemoglobin protein can carry four molecules of oxygen, which are delivered throughout the body by red blood cells. (medicalnewstoday.com)
- According to the Information Center for Sickle Cell and Thalassemic Disorders, hemoglobin bonds to oxygen molecules from the lungs and delivers them to cells throughout the body. (reference.com)
- As soon as the blood sample contacts the reagent on the membrane, the red blood cells are lysed and the hemoglobin molecules are released and dispersed into the membrane by the action of surfactant. (google.ca)
- Separation of hemoglobins is based on variable rates of migration of charged hemoglobin molecules in an electrical field. (medscape.com)
- In these organisms, hemoglobins may carry oxygen, or they may act to transport and regulate other small molecules and ions such as carbon dioxide, nitric oxide, hydrogen sulfide and sulfide. (wikipedia.org)
- Hemoglobin is found in red blood cells binding to four oxygen molecules in the lungs and transports them to the tissues. (kenyon.edu)
- Genetic sequences, binding characteristics and molecular structures of protoglobins were compared with those of hemoglobins and other oxygen-transport molecules from a wide range of organisms, including bacteria, tubeworms, roundworms, segmented "bloodworms," mice, humans and sperm whales. (innovations-report.com)
Forms of hemoglobin5
- Hemoglobin A1c was first separated from other forms of hemoglobin by Huisman and Meyering in 1958 using a chromatographic column . (wikipedia.org)
- The composition of the globin chain can vary, giving rise to several normal and abnormal forms of hemoglobin. (healthcentral.com)
- You may have this test if your health care provider suspects that you have a disorder caused by abnormal forms of hemoglobin ( hemoglobinopathy ). (medlineplus.gov)
- This course will update you on the laboratory testing that is currently being used to diagnose and differentiate between the various forms of hemoglobin S disorders. (medialab.com)
- Contributors examine the structure, expression, and evolution of the globin genes, the assembly of globin subunits into functional forms of hemoglobin, and the numerous variants that result from genetic alterations. (cshlpress.com)
Lungs20
- Haemoglobin in the blood carries oxygen from the lungs or gills to the rest of the body (i.e. the tissues). (wikipedia.org)
- Other cells that contain haemoglobin include the A9 dopaminergic neurons in the substantia nigra , macrophages , alveolar cells , lungs, retinal pigment epithelium, hepatocytes, mesangial cells in the kidney, endometrial cells, cervical cells and vaginal epithelial cells. (wikipedia.org)
- The principal function of hemoglobin is to combine and transport oxygen from the lungs following inhalation, and then deliver it to all body tissues, where it is required to provide energy for the chemical reactions of all living cells. (healthcentral.com)
- Hemoglobin (Hb) constitutes a vital link between ambient O2 availability and aerobic metabolism by transporting oxygen (O2) from the respiratory surfaces of the lungs or gills to the O2-consuming tissues. (nih.gov)
- The red respiratory protein of red blood cells that transports oxygen as oxyhemoglobin from the lungs to the tissues, where the oxygen is readily released and the oxyhemoglobin becomes hemoglobin. (dictionary.com)
- When the red blood cell carrying hemoglobin returns to the lungs, where oxygen concentration is high, the cycle of oxygen binding, transport, and release starts again. (dictionary.com)
- Hemoglobin transport is only one of a number of bodily mechanisms by which carbon dioxide travels from the tissues to the lungs for release to the air. (dictionary.com)
- Hemoglobin, which gives red blood cells their color, helps carry oxygen from the lungs to the rest of the body and carbon dioxide back to the lungs to be exhaled. (mayoclinic.org)
- Oxygen entering the lungs attaches to the hemoglobin in the blood, which carries it to the tissues in the body. (medicalnewstoday.com)
- The major function of hemoglobin is to transport oxygen from the lungs to the body's tissues and then transport carbon dioxide out of the tissue back to th. (reference.com)
- Haemoglobin, found in red blood cells, transports oxygen throughout the body from the lungs. (ehow.co.uk)
- In a typical total blood volume of 5 litres, even though more than half is in the veins, we thus have about 0.75 litre of oxygen combined with haemoglobin in the blood, and we have about the same amount as gas in the lungs. (encyclopedia.com)
- An example of hemoglobin is what brings oxygen from the lungs to the body's tissue. (yourdictionary.com)
- The iron-containing protein (pigment) found in red blood cells.Hemoglobin transports oxygen from the lungs to the body's tissues. (medindia.net)
- Hemoglobin transports oxygen from our lungs to the cells in our body. (blood.ca)
- Hemoglobin transports oxygen in the blood from the lungs to the rest of the body. (wikibooks.org)
- This is useful because, with a high affinity for oxygen in the lungs, hemoglobin can effectively bind to more oxygen. (wikibooks.org)
- It is said that 97 percent of the oxygen carried by the blood from the lungs is carried through haemoglobin and the other three percent is dissolved by the plasma. (ndtv.com)
- Hemoglobin, a protein found in red blood cells, carries oxygen from your lungs through your bloodstream to all of your cells. (livestrong.com)
- In humans, with each breath in, hemoglobin binds oxygen in the lungs. (innovations-report.com)
Anemia36
- Defects in hemoglobin production may be either genetic in origin (for example, sickle cell anemia) or acquired. (healthcentral.com)
- Anemia is a general term referring to a shortage of red blood cells or a reduction in hemoglobin. (healthcentral.com)
- If anemia is suspected, a simple blood test can be taken to detect a shortage of red blood cells or hemoglobin. (healthcentral.com)
- Any adult who has a hemoglobin content of less than 12 grams/100ml blood in women, and less than 13.5 grams/100 ml in men, is diagnosed as having anemia. (healthcentral.com)
- Iron deficiency anemia is caused by a shortage of the mineral iron, which is necessary to produce hemoglobin. (healthcentral.com)
- HbS is an abnormal form of hemoglobin associated with sickle cell anemia . (medlineplus.gov)
- Anemia is caused by an abnormal drop in either red blood cells or hemoglobin (the main constituent of red blood cells). (dictionary.com)
- A low hemoglobin count that's more severe and causes symptoms might mean you have anemia. (mayoclinic.org)
- EKF, announces the successful use of its FDA cleared DiaSpect Tm POC hemoglobin analyzer to study iron-deficient anemia in remote region of Ghana, West Africa. (news-medical.net)
- A large study just published in the journal Anaesthesia raises important questions about the way anemia is currently managed in surgical patients (Associations of nadir hemoglobin level and red blood cell transfusion with mortality and length of stay in surgical specialties: a retrospective cohort study). (news-medical.net)
- Findings from an interim analysis of a new study comparing the hemoglobin response rates of Epoetin alfa and darbepoetin alfa in the treatment of chemotherapy-related anemia were published in the November 15, 2004 issue of the Medical Journal 'Blood' as part of the American Society of Hematology 46th Annual Meeting and Exposition. (news-medical.net)
- Low hemoglobin levels usually indicate that a person has anemia. (medicalnewstoday.com)
- This form of anemia occurs when a person does not have enough iron in their body, and it cannot make the hemoglobin it needs. (medicalnewstoday.com)
- Two diseases that arise from mutations in the hemoglobin genes are sickle cell anemia and thalassemia. (reference.com)
- Hemoglobin is the protein in red blood cells that carry the oxygen your body needs throughout the blood stream and a low count is frequently a sign of anemia. (diabetesdaily.com)
- It then turns to functional abnormalities of whole blood in sickle cell anemia, inhibition of sickle hemoglobin gelation by amino acids and peptides, and intermolecular interactions in crystals of human deoxy hemoglobins A, C, F, and S. The chapters that follow focus on glycosylation of human hemoglobin, the phase transitions of sickle-cell hemoglobin, conformational effects of the HbS mutation, and mechanisms for hemoglobin oxidation. (elsevier.com)
- Problems with hemoglobin production cause common diseases, such as anemia, which comes from low levels of hemoglobin and is found in 25% of the world's population. (redorbit.com)
- Anemia can occur if the body's hemoglobin levels are too low. (brighthub.com)
- Mass spectrometry, a newer analytical technology, may be used to identify highly unstable hemoglobins that may manifest clinically as hemolytic anemia or thalassemia. (medscape.com)
- Sometimes your body does not contain adequate levels of hemoglobin, a condition known as anemia. (livestrong.com)
- Low hemoglobin levels lead to anemia, which causes symptoms like fatigue and trouble breathing. (clevelandclinic.org)
- Your healthcare provider can perform blood tests to check your hemoglobin level and to tell if you have anemia . (clevelandclinic.org)
- Sickle cell anemia (SCA) is a genetic blood disorder caused by abnormal inherited hemoglobin. (medindia.net)
- Anemia is defined as a hemoglobin level of less than 120 g/L in non-pregnant females and less than 130 g/L in males. (blood.ca)
- If anemia is present, you should not return to donate until the cause of the low hemoglobin has been identified and corrected. (blood.ca)
- Frequent blood donation can contribute to anemia because a "whole blood donation" results in a drop of hemoglobin levels by approximately 10 g/L. Healthy donors produce new red blood cells to replace donated cells. (blood.ca)
- There is an alternate test to measure fructosamine levels, which is sometimes used instead of the hemoglobin A1c test, for patients who require it, such as those with hemolytic anemia. (wisegeek.com)
- If your hemoglobin levels are too low, you may have anemia, which can leave your feeling fatigued or short of breath. (livestrong.com)
- Once your doctor determines the cause of your anemia, you'll be able to develop a treatment plan to raise hemoglobin levels. (livestrong.com)
- According to the National Anemia Action Council, the most common cause of low hemoglobin levels is an iron deficiency. (livestrong.com)
- Low hemoglobin levels may be one of the first signs of internal bleeding or other serious illness, such as sickle cell anemia. (livestrong.com)
- Although an iron deficiency is the most common cause of anemia, a B-12 deficiency or B-9 deficiency, also called folic acid, may cause low hemoglobin levels. (livestrong.com)
- When the amount of hemoglobin in the red blood cells drops below the required levels, based on the age and gender of the person, it leads to a disorder of the blood known as anemia . (home-remedies-for-you.com)
- Fewer red blood cells and lower hemoglobin levels may cause the person to develop anemia. (clevelandclinic.org)
- Anemia is a blood disorder that occurs when there is not enough hemoglobin in a person's blood. (clevelandclinic.org)
- Knowing this level may help doctors evaluate low concentrations of normal hemoglobin in red blood cells (anemia), as well as higher-than-normal levels of fetal hemoglobin or its hereditary persistence. (encyclopedia.com)
Fetal hemoglobin13
- fetal hemoglobin), hemoglobin C (HbC), and hemoglobin S (HbS). (medscape.com)
- Fetal hemoglobin (HbF) has two α- and two γ-globin chains (α 2 γ 2 ). (medscape.com)
- Also worth mentioning is the fact that fetal hemoglobin has a noticeably higher affinity for oxygen than does maternal hemoglobin. (wikibooks.org)
- Fetal hemoglobin, an alkali-resistant form of hemoglobin, is the major hemoglobin component in the bloodstream of the fetus. (encyclopedia.com)
- The determination of fetal hemoglobin in the blood of infants and children identifies normal and abnormal levels, defining what percentage of total hemoglobin is made up of fetal hemoglobin. (encyclopedia.com)
- Among the six types of hemoglobin, HbA is the normal adult hemoglobin, and HbF is the major fetal hemoglobin. (encyclopedia.com)
- During fetal development, fetal hemoglobin composes about 90 percent of total hemoglobin. (encyclopedia.com)
- At birth, the newborn's blood is composed of about 70 percent fetal hemoglobin. (encyclopedia.com)
- As the infant's bone marrow begins to produce new red cells, fetal hemoglobin begins to decrease rapidly. (encyclopedia.com)
- In some diseases associated with abnormal hemoglobin production (hemoglobinopathy), fetal hemoglobin may persist in larger amounts. (encyclopedia.com)
- When this occurs, the increased amounts of fetal hemoglobin raise questions of possible underlying dysfunction or disease. (encyclopedia.com)
- Persistence of fetal hemoglobin in inherited hemolytic anemias can be associated with less severe disease symptoms. (encyclopedia.com)
- Testing for levels of fetal hemoglobin and other types of hemoglobin may be a first, important step in the investigation of possible hemoglobinopathies. (encyclopedia.com)
Type of hemoglobin6
- The most common type of hemoglobin in mammals contains four such subunits. (wikipedia.org)
- This group of genetic blood diseases affects the amount and type of hemoglobin made (for example, too much hemoglobin F and not enough hemoglobin A in a child). (kidshealth.org)
- The hemoglobins move on the paper and form bands that show the amount of each type of hemoglobin. (medlineplus.gov)
- This is the main type of hemoglobin in an unborn baby's body. (medlineplus.gov)
- And what I mean by that is, thinking specifically about the type of hemoglobin. (khanacademy.org)
- Most people who are heterozygous - having one variant gene and one standard hemoglobin gene - for a hemoglobin variant have no symptoms and may not know that they carry this type of hemoglobin. (diabetesincontrol.com)
Form of hemoglobin10
- Glycated hemoglobin ( hemoglobin A1c , HbA1c , A1C , or less commonly HgbA1c, haemoglobin A1c, HbA 1c , Hb1c, etc.) is a form of hemoglobin that is bound to glucose. (wikipedia.org)
- In the method, a specific binding partner to the first form of hemoglobin is added to the sample, and the sample is then subjected to. (google.com)
- c) determining the content of the first form of hemoglobin in the sample from the electropherogram. (google.com)
- 2. The method of claim 1 wherein the first form of hemoglobin is a glycosylated hemoglobin. (google.com)
- f) determining the absolute concentration of the first form of hemoglobin in the sample from a standard curve of protein concentration versus the ratio of protein signal to internal standard signal. (google.com)
- 8. The method of claim 7 wherein the first form of hemoglobin is Hb A 1c . (google.com)
- There is more than one hemoglobin gene: in humans, hemoglobin A (the main form of hemoglobin present) is coded for by the genes, HBA1, HBA2, and HBB. (wikipedia.org)
- Hemoglobin Gower 1 (also referred to as ζ2ε2 or HbE Gower-1) is a form of hemoglobin existing only during embryonic life, and is the primary embryonic hemoglobin. (wikipedia.org)
- Hemoglobin Gower 2 (also referred to as α2ε2 or HbE Gower-2) is a form of hemoglobin existing at low levels during embryonic and fetal life. (wikipedia.org)
- Hemoglobin Portland I (also referred to as ζ2γ2 or HbE Portland-1) is a form of hemoglobin existing at low levels during embryonic and fetal life, composed of two zeta chains and two gamma chains. (wikipedia.org)
20192
- Cite this: Hemoglobin A1c Misses Many Cases of Diabetes - Medscape - Mar 27, 2019. (medscape.com)
- The Global market size of Glycosylated Hemoglobin and C-Peptide Market was $XX million in 2019 with XX CAGR, and it is expected to reach $XX million by the end of 2026 with a CAGR of XX% from 2019 to 2026. (openpr.com)
Protein in red blood5
- Hemoglobin is a protein in red blood cells that carries oxygen. (medlineplus.gov)
- A high hemoglobin count indicates an above-normal level of the iron-containing protein in red blood cells. (mayoclinic.org)
- Hemoglobin is an iron-rich protein in red blood cells. (medicalnewstoday.com)
- Hemoglobin is the oxygen-carrying protein in red blood cells. (encyclopedia.com)
- Hemoglobin is an iron-containing protein in red blood cells that transports oxygen to tissues throughout the body. (cshlpress.com)
Variants6
- Hemoglobin variants and hemoglobin A1c analysis: problem solved? (medscape.com)
- 4. The method of claim 3 wherein the macromolecular specific binding partner is an antibody that specifically binds Hb A 1c and lacks significant binding affinity for Hb A and other hemoglobin variants. (google.com)
- According to the NGSP - The hemoglobin A1C (A1C) test can be unreliable for diagnosing or monitoring diabetes and prediabetes in people with inherited hemoglobin variants, also called hemoglobinopathies. (diabetesincontrol.com)
- Hemoglobins S and E are prevalent variants in people of African, Mediterranean, or Southeast Asian descent. (diabetesincontrol.com)
- Reliable A1C tests that do not cause interference with hemoglobin variants are available. (diabetesincontrol.com)
- Even within a species, different variants of hemoglobin always exist, although one sequence is usually a "most common" one in each species. (wikipedia.org)
Total hemoglobin13
- Certain diseases are associated with high HbF levels (when HbF is more than 2% of the total hemoglobin). (medlineplus.gov)
- We showed that intrinsic total hemoglobin contrast holds promise as an adjunct to diagnostic mammography and ultrasound for distinguishing early-stage invasive breast cancers from benign lesions," they added. (medpagetoday.com)
- The total hemoglobin contrast may also help to distinguish some high-risk proliferative lesions from nonproliferative lesions. (medpagetoday.com)
- Light absorption was measured at two optical wavelengths, and lesion angiogenesis was calculated from total hemoglobin concentration and compared with biopsy results. (medpagetoday.com)
- Women found to have malignant lesions underwent excision, and total hemoglobin was compared with pathologic parameters. (medpagetoday.com)
- The in situ and T1 lesions had mean and mean maximal total hemoglobin values of 71.9 and 102.0 µmol/L, respectively. (medpagetoday.com)
- For large ultrasound-visible lesions, this technique can provide some total hemoglobin distribution features, such as heterogeneous peripheral enhancement and/or posterior shadowing, that can add diagnostic value to ultrasound," Zhu and colleagues wrote. (medpagetoday.com)
- In addition, the total hemoglobin distribution can be monitored and used to assess response in patients who have locally advanced cancers and who are undergoing neoadjuvant chemotherapy. (medpagetoday.com)
- Because the amount of oxygen dissolved in the sample is known, the total hemoglobin is determined by subtracting the amount of free oxygen from the total oxygen measured, recognizing the fast equilibrium Hb+O 2 ⇄HbO 2 . (google.com)
- The present invention relates to a process for the determination of the amount of irreversibly glycated hemoglobin, or HbA1c, present in a sample of blood, relative to the amount of total hemoglobin. (google.com)
- in adulthood, only traces (0.5% or less) are found in total hemoglobin. (encyclopedia.com)
- The invention provides enzymatic methods for direct determination of percentage of glycated hemoglobin in blood samples without the need of a separated measurement of total hemoglobin content in blood samples. (google.com.au)
- c) determining percentage of glycated hemoglobin A1c in the sample by correlating the measured value from the generated signal in step b) to a percentage of glycated hemoglobin A1c in a calibration curve without measuring the total hemoglobin in the blood sample separately. (google.com.au)
Globin12
- The name hemoglobin is derived from the words heme and globin , reflecting the fact that each subunit of hemoglobin is a globular protein with an embedded heme group. (wikipedia.org)
- Hemoglobin is a crystallizable, conjugated protein consisting of an iron-containing pigment (called heme or hematin) and a simple protein, globin. (healthcentral.com)
- Hemoglobin comprises two major parts: a protein-complex called globin and four heme groups. (reference.com)
- The globin chain of hemoglobin is broken down into amino acids that are either metabolized by the macrophages or absorbed by the bloodstream. (reference.com)
- The alpha globin obtained from the E. coli expressed hemoglobin was also combined with normal human beta chains and hemin to form the alphaV1M variant. (rcsb.org)
- Hemoglobin is a tetramer with two pairs of globin chains, each containing an identical heme group. (medscape.com)
- Normal adult hemoglobin (HbA) has two α- and two β-globin chains (α 2 β 2 ). (medscape.com)
- Minor adult hemoglobin (HbA 2 ) is made of two α- and two δ-globin chains (α 2 δ 2 ). (medscape.com)
- The amino acid sequences of the globin proteins in hemoglobins usually differ between species. (wikipedia.org)
- For example, the most common hemoglobin sequences in humans and chimpanzees are nearly identical, differing by only one amino acid in both the alpha and the beta globin protein chains[citation needed]. (wikipedia.org)
- Hemoglobin consists primarily of iron-bearing proteins called heme groups and moiety globin protein, which together give hemoglobin its ability to carry oxygen. (encyclopedia.com)
- To produce hemoglobin S, glutamic acid that is normally present in the sixth position on the beta globin chain is substituted with which of the follow. (medialab.com)
Glucose19
- Normal levels of glucose produce a normal amount of glycated hemoglobin. (wikipedia.org)
- As the average amount of plasma glucose increases, the fraction of glycated hemoglobin increases in a predictable way. (wikipedia.org)
- In diabetes mellitus , higher amounts of glycated hemoglobin, indicating poorer control of blood glucose levels, have been associated with cardiovascular disease , nephropathy , neuropathy , and retinopathy . (wikipedia.org)
- The use of hemoglobin A1c for monitoring the degree of control of glucose metabolism in diabetic patients was proposed in 1976 by Anthony Cerami , Ronald Koenig and coworkers. (wikipedia.org)
- Doctors order blood tests to check things such as the levels of glucose , hemoglobin, or white blood cells. (kidshealth.org)
- NEW YORK (Reuters Health) - The hemoglobin A1c blood test used widely to diagnose diabetes is "highly unreliable" with a significant tendency to miss cases of diabetes and overestimate the prevalence of normal glucose tolerance (NGT), according to new research. (medscape.com)
- Clinicians "should not rely solely" on hemoglobin A1c, and perhaps for high-risk patients should "pursue oral glucose-tolerance test to further elucidate a diagnosis," Dr. Maria Mercedes Chang Villacreses said during a press briefing at The Endocrine Society's annual meeting in New Orleans, where the findings were presented March 23. (medscape.com)
- However, in an effort to smooth the transition to the new units, as well as to help both physicians and patients appreciate the clinical context of various hemoglobin A1c levels, many laboratories are now reporting eAG (estimated average glucose) along with every hemoglobin A1c level. (medscape.com)
- Chan CL, Pyle L, Newnes L, Nadeau KJ, Zeitler PS, Kelsey MM. Continuous glucose monitoring and its relationship to hemoglobin A1c and oral glucose tolerance testing in obese and prediabetic youth. (medscape.com)
- a stable glycoprotein formed when glucose binds to hemoglobin A in the blood Blood sugar was assessed by measuring the amount of hemoglobin A1c in the participants' blood, a test that looks for hemoglobin with sugar attached to it. (merriam-webster.com)
- HbA1c is formed as a result of binding of glucose with hemoglobin present in red blood cells. (medindia.net)
- Glycated Hemoglobin (HbA1c or A1c) Calculator calculates average blood glucose level, which is directly related to HbA1c. (medindia.net)
- Unlike using a blood glucose meter - which captures your sugar levels at a given point in time , the Hemoglobin A1c test captures your body's sugar level over a three month period. (howstuffworks.com)
- HbA1c is a glycated hemoglobin formed by a binding reaction between an amine group of hemoglobin and the glucose aldehyde group, for example between the amino group of the N-terminal valine of the β-chain of hemoglobin and the glucose aldehyde group. (google.com)
- The percentage of HbA1c (i.e. the amount of glycated hemoglobin relative to total hemaglobin in the blood) has come to be taken as a measure of the level of blood glucose control a diabetic patient has maintained for a period of two or three months prior to the measurement. (google.com)
- At any given average glucose level, high variability results in higher glycosylated hemoglobin level. (diabetesincontrol.com)
- It is possible that low hemoglobin A1c test results indicate a mix of incidents of high blood glucose and hypoglycemia. (wisegeek.com)
- As a person's blood sugar gets higher, glucose attaches to hemoglobin (a substance inside red blood cells that carries oxygen to cells). (rchsd.org)
- The glucose remains attached to the hemoglobin for the life of the red blood cell, or about 2 to 3 months. (rchsd.org)
Tissues9
- In these tissues, haemoglobin has a non-oxygen-carrying function as an antioxidant and a regulator of iron metabolism . (wikipedia.org)
- The enriched hemoglobin circulates and is carried through the body to the tissues, where the nitric oxide dilates the small capillaries, allowing hemoglobin to deliver its oxygen to the tissues. (infoplease.com)
- In this way, hemoglobin stops itself from competing with the tissues for needed oxygen. (dictionary.com)
- Haemoglobin not only distributes oxygen as it is required by the tissues but is also an important store of the gas. (encyclopedia.com)
- As oxygen pressure reduces below that required for full saturation, haemoglobin is relatively little desaturated until and unless the oxygen pressure reaches about the level which blood normally encounters in the oxygen-using tissues: it then parts with it readily. (encyclopedia.com)
- deoxygenated hemoglobin accessorizes a feedback loop by reducing nitrite to NO, a vasodilator which enhances blood flow to oxygen-deprived tissues. (mpbio.com)
- When hemoglobin levels are low, your tissues and organs do not receive enough oxygen. (livestrong.com)
- Once it reaches the muscle, where the pH is lower, the lowered affinity for oxygen allows hemoglobin to release its oxygen into the tissues. (wikibooks.org)
- Red blood cells deliver hemoglobin throughout the body, ensuring that all body tissues have the oxygen they need for life and proper function. (encyclopedia.com)
Thalassemia2
- Doctors may order the test to help diagnose conditions related to irregular hemoglobin production, such as sickle cell disease or thalassemia. (kidshealth.org)
- Due to its relative stability compared to hemoglobin Gower 1 and hemoglobin S, it has been proposed as a subject for reactivation in the adult in cases of severe β thalassemia and hemoglobinopathies in subjects for which the reactivation of hemoglobin F is contraindicated due to toxicity concerns. (wikipedia.org)
Structure of hemoglobin6
- In 1959, Max Perutz determined the molecular structure of hemoglobin by X-ray crystallography . (wikipedia.org)
- Normally, iron binds with oxygen to form rust (iron oxide), but the structure of hemoglobin prevents this from happening, since it would inactivate the heme subunits. (dictionary.com)
- The glycine crosslinks, localized between one N- and C--termini pair of the alpha subunits in the deoxy crystalline state, do not perturb the overall tertiary or quaternary or even the local structure of hemoglobin. (rcsb.org)
- The 3D structure of hemoglobin, PDB ID 1hho . (wikibooks.org)
- The three-dimensional structure of hemoglobin was solved using X-ray crystallography in 1959 by Max Perutz. (wikibooks.org)
- The structure of hemoglobin is very similar to the single polypeptide chain in myoglobin despite the fact that their amino acid sequences differ at 83% of the residues. (wikibooks.org)
Tetramer3
- Therefore, genetic fusion to prevent the dissociation of the hemoglobin tetramer, thereby inhibiting renal clearance based upon molecular size, is a structurally conservative method to stabilize hemoglobin for use as an oxygen-delivery therapeutic. (rcsb.org)
- Hemoglobin ( Haemoglobin in many varieties of English and often abbreviated to 'Hb') is a tetramer consisting of two dimers that bind to oxygen. (wikibooks.org)
- Embryonic hemoglobin is a tetramer produced in the blood islands in the embryonic yolk sac during the mesoblastic stage (first week of pregnancy until the end of the pregnancy). (wikipedia.org)
Subunits3
- Carbon dioxide does not bind the heme in hemoglobin, but rather the amino groups at the ends of the hemoglobin's protein subunits. (dictionary.com)
- The process whereby hemoglobin performs this essential physiological role is characterized by a cooperative interaction among its constituent subunits. (springer.com)
- The human hemoglobin protein is made up of four subunits, two identical alpha subunits ( A and C , 141 residues) and two identical beta subunits ( B and D , 146 residues). (kenyon.edu)
HbA1c3
- Both the glycoprotein and the test are also called A1c , glycated hemoglobin , glycohemoglobin , glycosylated hemoglobin , HA1c , and HbA1c . (merriam-webster.com)
- Glycated/Glycosylated Hemoglobin ( HbA1c ) test checks your average blood sugar level in the past 3 months. (medindia.net)
- This report analyzes the worldwide markets for Hemoglobin A1c Monitoring in US$ by the following Test Types: HbA1c Laboratory Testing, and HbA1c Point of Care Testing. (reportlinker.com)
Adult hemoglobin4
- So we know that the adult hemoglobin has four units to it. (khanacademy.org)
- So let me draw the adult hemoglobin over here on the left. (khanacademy.org)
- Let me just first write out adult hemoglobin. (khanacademy.org)
- And there isn't one type of adult hemoglobin. (khanacademy.org)
Proteins2
- After the removal of unbound proteins by washing, anti-Hemoglobin antibodies conjugated with horseradish peroxidase (HRP), are added. (abcam.com)
- Red-blooded genealogists take note: The discovery in microbes of two oxygen-packing proteins, the earliest known ancestors to hemoglobin, brings scientists closer to identifying the earliest life forms to use oxygen. (innovations-report.com)
Levels65
- High hemoglobin level is most often caused by low oxygen levels in the blood (hypoxia), present over a long period of time. (medlineplus.gov)
- However, if your child has had a transfusion in the last 3 months, hemoglobin levels may be altered, so let the doctor know. (kidshealth.org)
- What is the cause of the low hemoglobin levels? (healthcentral.com)
- What's to know about hemoglobin levels? (medicalnewstoday.com)
- Here, we will look at the role of hemoglobin, and how levels of it in the blood are tested. (medicalnewstoday.com)
- How are hemoglobin levels tested? (medicalnewstoday.com)
- Hemoglobin levels are measured by a blood test. (medicalnewstoday.com)
- High hemoglobin levels could be indicative of the rare blood disease, polycythemia. (medicalnewstoday.com)
- Here is a list of the most common causes of elevated haemoglobin levels. (ehow.co.uk)
- A simple blood test is all it takes to find out if your haemoglobin levels are normal. (ehow.co.uk)
- If you are dehydrated at the time of the test, your haemoglobin levels may be falsely elevated. (ehow.co.uk)
- If this is the case, haemoglobin levels will return to normal upon proper hydration. (ehow.co.uk)
- Although the mechanism hasn't quite been worked out, smokers have a tendency to have elevated haemoglobin levels. (ehow.co.uk)
- Injecting erythropoietin (EPO) to enhance athletic performance can also cause high haemoglobin levels. (ehow.co.uk)
- The fact that this medication, which stimulates the production of red blood cells, is used to treat anaemia is a sure sign that it can raise the haemoglobin levels of a healthy person to excess. (ehow.co.uk)
- Less commonly, high haemoglobin levels are caused by more serious conditions. (ehow.co.uk)
- Other types of heart and lung diseases in addition to exposure to toxins are all possible (but rare) causes of elevated haemoglobin levels. (ehow.co.uk)
- C peptide levels, B12 & Hemoglobin levels high. (diabetesdaily.com)
- This new finding is critical: understanding how hemoglobin levels are controlled at a genetic level has significant public health implications for people of all ages in developing and developed countries", explains Dr John Chambers, from the Department of Epidemiology and Public Health at Imperial College London and one of the lead authors of the study. (redorbit.com)
- Changes in hemoglobin levels can also affect our susceptibility to diseases like malaria, which infect the red blood cells" says Professor Kooner, from the National Heart and Lung Institute at Imperial College London and the study's chief investigator. (redorbit.com)
- The new research adds to our understanding of the multiple causes of problems with hemoglobin levels, which include an iron-deficient diet, chronic diseases such as cancer, and genetic associations, such as the one described in this paper. (redorbit.com)
- In the future, the finding could lead to new treatments for people suffering from chronic problems with hemoglobin levels not linked to iron in the diet. (redorbit.com)
- Designing a drug that enhances TMPRSS6 activity could augment hemoglobin in people such as cancer and kidney failure patients, who suffer from chronically low levels. (redorbit.com)
- A different drug that blocked TMPRSS6 enzyme production might bring down high hemoglobin levels", adds Dr Chambers. (redorbit.com)
- This test measures the body's blood levels of hemoglobin. (brighthub.com)
- When the hemoglobin levels in the blood are elevated, polycythemia vera can occur. (brighthub.com)
- Many environmental factors and poor health decisions can cause hemoglobin levels to rise. (brighthub.com)
- One reason a test may be done to measure hemoglobin levels is to monitor previous medical conditions. (brighthub.com)
- Testing hemoglobin levels can also be used to view a persons overall health. (brighthub.com)
- Monitoring the bloods hemoglobin levels can help test for many medical disorders. (brighthub.com)
- The test for measuring hemoglobin levels is relatively simple. (brighthub.com)
- Diabetes screening is done using blood tests like fasting blood sugar and hemoglobin A1c levels. (medindia.net)
- Low hemoglobin levels may leave you feeling more tired than usual during exercise. (livestrong.com)
- Do Certain Foods Raise Hemoglobin Blood Levels? (livestrong.com)
- AMSTERDAM -- High levels of hemoglobin may be dangerous in patients with nonalcoholic fatty liver disease (NAFLD), with bleeding a potential remedy, researchers said here. (medpagetoday.com)
- Some research has linked hemoglobin levels to the level of liver damage in NAFLD patients, as well as suggesting that excess iron may be overtly hepatotoxic -- that is, not just an epiphenomenon in NAFLD. (medpagetoday.com)
- High hemoglobin levels were associated with younger patient age, higher blood lipid levels, and increased ALT and AST, Peltec and colleagues reported. (medpagetoday.com)
- Normal hemoglobin levels are different in women and in men. (blood.ca)
- Why does Canadian Blood Services measure hemoglobin levels? (blood.ca)
- Donating blood with low hemoglobin levels may cause you to become anemic. (blood.ca)
- We recommend that you see your doctor to check your hemoglobin levels and iron stores (ferritin). (blood.ca)
- If your doctor has started you on iron pills, you may return to donate six months after starting them, if your hemoglobin and iron levels are back to normal. (blood.ca)
- What steps can I take to improve my hemoglobin levels? (blood.ca)
- As per Nutritionist Sujetha Shetty, "Consuming foods that are rich in iron, folic acid and vitamin B-12 help in maintaining haemoglobin levels. (ndtv.com)
- As per the National Anaemia Action Council, iron deficiency is one of the most common causes of low haemoglobin levels. (ndtv.com)
- Drink pomegranate juice daily in order to ensure your haemoglobin levels are at par. (ndtv.com)
- Dates provide ample sources of iron that increases haemoglobin levels in the blood. (ndtv.com)
- Beetroot is one of the best ways to increase haemoglobin levels. (ndtv.com)
- His haemoglobin level has risen and carbon-dioxide levels have come down, but he will continue to need oxygen," she added. (ndtv.com)
- The hemoglobin A1c (A1c) test is a measure of blood sugar levels that is more reliable than the standard finger prick test performed at home, using a blood sugar meter. (wisegeek.com)
- If sugar levels are high in the blood, they will bind to hemoglobin. (wisegeek.com)
- The hemoglobin A1c test provides a reliable measure of blood sugar levels over the past three months, which is the approximate lifespan of a red blood cell. (wisegeek.com)
- Since it measures the amount of glycated hemoglobin in the red blood cells, the hemoglobin A1c test provides an estimate of blood sugar levels over the preceding months. (wisegeek.com)
- One might expect that low levels from a hemoglobin A1c test would be considered healthy for a diabetic, but this may not be the case. (wisegeek.com)
- It will take your body a week to start manufacturing more red blood cells and hemoglobin levels should rise within three weeks. (livestrong.com)
- Stomach ulcers and heavy menstrual bleeding can also cause low hemoglobin levels. (livestrong.com)
- Treat the underlying cause of your low hemoglobin to stabilize hemoglobin levels. (livestrong.com)
- Iron is responsible in determining the blood's hemoglobin levels. (home-remedies-for-you.com)
- Nutritional deficiency, particularly the deficiency of iron, vitamin B12 or folic acid, is the most common cause of low levels of hemoglobin in the blood. (home-remedies-for-you.com)
- There are several natural remedies that can increase the levels of hemoglobin in the red blood cells. (home-remedies-for-you.com)
- Eat ripe bananas, as they are rich in iron and bananas mixed with honey twice daily are believed to increase the levels of hemoglobin. (home-remedies-for-you.com)
- Hence, individuals afflicted with low levels of hemoglobin are recommended to add foods with a high content of Vitamin C in their diets. (home-remedies-for-you.com)
- This will also raise your hemoglobin levels very rapidly. (home-remedies-for-you.com)
- Human Hemoglobin ELISA Kit is an in vitro enzyme-linked immunosorbent assay (ELISA) for the quantitative measurement of Hemoglobin levels in human serum and plasma. (abcam.com)
- If a disease or condition affects the body's production of red blood cells, the hemoglobin levels may drop. (clevelandclinic.org)
Binds4
- Hemoglobin is the iron-carrying protein found in red blood cells that binds to oxygen. (healthcentral.com)
- To cope, the body produces extra haemoglobin so it can maximise the amount of oxygen it binds to. (ehow.co.uk)
- The conformation of hemoglobin also changes as the oxygen binds to the iron, raising both the iron and the histidine residue bound to it. (wikibooks.org)
- Once sugar binds to the hemoglobin, it stays bound. (wisegeek.com)
Diabetes6
- Hemoglobin A1c has become the primary method of screening and diagnosing diabetes. (medscape.com)
- Impact of common genetic determinants of Hemoglobin A1c on type 2 diabetes risk and diagnosis in ancestrally diverse populations: A transethnic genome-wide meta-analysis. (nih.gov)
- For any diabetic, the Hemoglobin A1c test will help you and your doctor to better manage your diabetes. (howstuffworks.com)
- Most people who have diabetes should keep their hemoglobin A1c under seven percent . (howstuffworks.com)
- The hemoglobin A1c test is an important part of your diabetes management plan and can help you tell whether your plan is working. (howstuffworks.com)
- Hemoglobin A1c in Diabetes: Panacea or Pointless? (diabetesjournals.org)
Measure hemoglobin3
- Does anybody know why I should measure hemoglobin release at 540 nm in stead of 430 nm? (bio.net)
- It utilizes a BMEYE finger cuff to capture and continuously measure beat-to-beat blood pressure (sys/dia), mean arterial pressure (MAP), cardiac output (CO), stroke volume (SV), systemic vascular resistance (SVR), and derivative of pressure (dP/dt), and a Masimo finger sensor to noninvasively and continuously measure hemoglobin (SpHb(R)), oxygen saturation (SpO2), oxygen content (SpOC(TM)), and perfusion index (PI). (medgadget.com)
- We measure hemoglobin to protect you as a donor, and to ensure the quality of the red blood cells that will be transfused into blood recipients. (blood.ca)
Amount of glycated hemoglobin2
- This can be followed by determining the amount of glycated hemoglobin in the sample. (google.com)
- an electrochemical cell comprising cathode for electrochemically determining a total amount of hemoglobin and/or an amount of glycated hemoglobin in the sample, and an anode, the cathode comprising an enzyme capable of reducing oxygen to water. (google.com)
Percentage of glycated hemoglobin1
- A method of determining the percentage of glycated hemoglobin in a blood sample is disclosed wherein at least one of the assay steps is performed electrochemically. (google.com)
Human hemoglobins1
- The crystal structures of three recombinant human hemoglobins, rHb1. (rcsb.org)
Disorders4
- The thalassemias are a group of genetic blood disorders that affect a person s ability to produce hemoglobin. (medindia.net)
- However, they are not present in all hemoglobin S disorders, or may not be present in all stages of a disorder. (medialab.com)
- The pathophysiological consequences of hemoglobin disorders (e.g., ineffective erythropoiesis and aberrant iron homeostasis), their clinical manifestations, and epidemiological trends are also described. (cshlpress.com)
- This book includes discussions of management and treatment strategies for hemoglobin disorders, such as transfusions, iron-chelating agents, gene therapy, and stem cell transplantation. (cshlpress.com)
Grams8
- A healthy individual has 12 to 16 grams of haemoglobin in every 100 ml of blood. (wikipedia.org)
- The amount of hemoglobin in the blood averages between 12 and 16 grams/100 milliliters of blood in adult females, about 14 and 18 in males, and somewhat less in children. (healthcentral.com)
- A low hemoglobin count is generally defined as less than 13.5 grams of hemoglobin per deciliter (135 grams per liter) of blood for men and less than 12 grams per deciliter (120 grams per liter) for women. (mayoclinic.org)
- It's generally defined as more than 17.5 grams (g) of hemoglobin per deciliter (dL) of blood for men and 15.5 g/dL for women. (mayoclinic.org)
- Hemoglobin, or Hb, is usually expressed in grams per deciliter (g/dL) of blood. (medicalnewstoday.com)
- 1. A pharmaceutical composition for transporting and releasing oxygen comprising a suspension of from about 5 to about 20 grams of reduced lesion hemoglobin per deciliter of a pharmaceutically acceptable carrier. (freepatentsonline.com)
- Hemoglobin is considered low if it is less than 13 grams per deciliter, or g/dL, for men and 12 g/dL for women. (livestrong.com)
- According to Sujetha Shetty, Nutritionist at Gympik.com, "Ideally a male needs 13.5 to 17.5 grams per decilitre and female needs 12.0 to 15.5 grams per decilitre haemoglobin that is deemed as normal. (ndtv.com)
Types of hemoglobin2
- Normal hemoglobin carries and delivers oxygen well, but some abnormal types of hemoglobin do not. (kidshealth.org)
- Many different types of hemoglobin (Hb) exist. (medlineplus.gov)
Concentration8
- of this is hemoglobin (mean corpuscular hemoglobin concentration, or MCHC, normally is 32 to 36 percent). (britannica.com)
- A chapter that assesses the effect of physiological parameters, such as pH, oxygen concentration, protein concentration, non-gelling hemoglobins, and the erythrocyte membrane, on the kinetics of polymerization of deoxyhemoglobin S concludes the book. (elsevier.com)
- the average hemoglobin concentration in a given volume of packed red blood cells, calculated from the hemoglobin therein and the hematocrit, in erythrocyte indices. (drugs.com)
- The reflection is inversely proportional to hemoglobin concentration. (google.ca)
- The intensity of the reflected light is converted to hemoglobin concentration, g/dL, or mmol/L by an interpolative comparison with stored reflection data indicative of known hemoglobin contents. (google.ca)
- To maintain a material balance hemoglobin must then diffuse back and can carry small amounts of oxygen against a concentration gradient of oxygen. (springer.com)
- Cell specialised for oxygen transport, having a high concentration of hemoglobin in the cytoplasm. (medindia.net)
- thus, the absorbance, at 450 nm, is a measure of the concentration of Hemoglobin in the test sample. (abcam.com)
Measurement3
- The apparatus and method for quickly measuring the hemoglobin content of a sample of blood uses a light reflectance measurement of the hemoglobin sample lysed in a membrane. (google.ca)
- Murine monoclonal antibodies against human normal and variant hemoglobins may be used for identification and/or quantification of hemoglobins, such as HbF measurement with radial immunodiffusion or HbF-containing erythrocytes (F-cells) with flow cytometry. (medscape.com)
- Hemoglobin measurement at 540nm or 430nm? (bio.net)
Sickle Cell Hemoglobin2
- Contributors discuss the biochemical and clinical aspects of hemoglobin abnormalities and cover topics ranging from amino acid substitutions to sickle cell disease, glycosylated hemoglobins, cystamine inhibition of sickling, and gelation of sickle cell hemoglobin. (elsevier.com)
- Interpret laboratory results for sickle cell hemoglobin case studies. (medialab.com)
Nitric oxide2
- Members of the hemoglobin superfamily efficiently catalyze nitric-oxide dioxygenation, and when paired with native electron donors, function as NO dioxygenases (NODs). (hindawi.com)
- Hemoglobin can also bind to carbon monoxide and nitric oxide. (kenyon.edu)
Level17
- How long does it take with diet alone to increase the hemoglobin level? (healthcentral.com)
- my family members say this is due to the less hemoglobin level. (medhelp.org)
- help me out with what food will be good for rising the hemoglobin level? (medhelp.org)
- A low level of hemoglobin in the blood relates directly to a low level of oxygen. (medicalnewstoday.com)
- What Is a Normal Hemoglobin Level? (reference.com)
- A low haemoglobin level, a condition known as anaemia, is fairly common and has serious effects. (ehow.co.uk)
- A gene with a significant effect on regulating hemoglobin in the body has been identified as part of a genome-wide association study, which looked at the link between genes and hemoglobin level in 16,000 people. (redorbit.com)
- In another study, elevated hemoglobin level appeared to adversely influence the cardiovascular risk profile in patients with NAFLD. (medpagetoday.com)
- A modified diet rich in Folate, Vitamin B12 and Iron is essential for the rapid rise in hemoglobin level. (medindia.net)
- It is important that you do not donate blood if your hemoglobin level is low. (blood.ca)
- We check each donor's hemoglobin level at the clinic before every donation with an onsite finger stick test. (blood.ca)
- If your hemoglobin level is below 110 g/L, you should see your physician for further testing. (blood.ca)
- Most people who have low hemoglobin are able to improve their iron level and hemoglobin count and become eligible donors once again, provide that they meet all other eligibility criteria. (blood.ca)
- A folic acid deficiency may lead to a low haemoglobin level. (ndtv.com)
- Is it possible that hypoglycemia increases the hemoglobin level? (wisegeek.com)
- Recent studies have shown that the level of hemoglobin in the body can be boosted by foods rich in iron. (home-remedies-for-you.com)
- Bananas too have been found to be quite beneficial in increasing the level of hemoglobin. (home-remedies-for-you.com)
Genes1
- The heme groups are molecular chains of different types and actually create six different hemoglobins that vary in their amino acid composition and also in the genes that control them. (encyclopedia.com)
Deficiency2
- This is a deficiency of hemoglobin , or red corpuscles, or both. (dictionary.com)
- One of the most common conditions that humans tend to suffer from is deficiency of haemoglobin . (ndtv.com)
Carry oxygen3
- The red color of blood comes from the hemoglobin that makes up the majority of the mass of the cell, which allows the blood cell to carry oxygen around the. (reference.com)
- Hemoglobin is needed in the body to carry oxygen through out the body. (brighthub.com)
- Hemoglobin is a substance in red blood cells that makes it possible for blood to transport (carry) oxygen throughout the body. (clevelandclinic.org)
Glycosylated hemoglobin in the b1
- This blood test measures the amount of glycosylated hemoglobin in the blood. (rchsd.org)
Measuring the hemoglobin content1
- Explain to patients that measuring the hemoglobin content of breast masses using optical tomography may help distinguish between benign and malignant lesions. (medpagetoday.com)
Bind3
- Healthy humans have about 15 g of haemoglobin per litre of blood, and this can bind with 200 ml of oxygen per litre. (encyclopedia.com)
- Early hemoglobins most likely evolved to bind and detoxify these gases. (innovations-report.com)
- When oxygen became a component of the atmosphere, it was also toxic, and these early organisms used hemoglobin to bind and ultimately detoxify the oxygen. (innovations-report.com)
Dissolved oxygen in blood1
- Haemoglobin has an oxygen-binding capacity of 1.34 mL O 2 per gram, which increases the total blood oxygen capacity seventy-fold compared to dissolved oxygen in blood. (wikipedia.org)
Biochemistry3
- 1992) Biochemistry 31, 8619-has been transformed into a functionally homogeneous protein whose properties closely approximate those of normal hemoglobin A. (rcsb.org)
- 1992) Biochemistry 31, 8619-has been transformed into a functionally homogeneous protein whose properties closely approximate those of normal hemoglobin A. Both of the alpha and beta chains of this hemoglobin contain a valine-methionine substitution at position 1 in order to accommodate the difference in specificity of the protein-processing enzymes of procaryotes. (rcsb.org)
- The focus of research of the Biochemistry of Hemoglobin (Hb)-based Substitutes Section is on the structural-functional characterization of modified Hb in relation to its redox (reduction-oxidation) chemistry and toxicity. (fda.gov)
Gene2
- It shows a strong association between a gene known as TMPRSS6 and the regulation of hemoglobin. (redorbit.com)
- Hemoglobin is used to study paradigm for the regulation of gene expression and cellular differentiation. (mpbio.com)
Test14
- 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 low hemoglobin count is a commonly seen blood test result. (mayoclinic.org)
- Hemoglobin tests are usually conducted to test the blood for the amount of hemoglobin present in the blood. (brighthub.com)
- Hemoglobin test are often given to test for underlying health conditions. (brighthub.com)
- Why is a Hemoglobin Test Used? (brighthub.com)
- In order to diagnose many medical conditions, a hemoglobin test is often conducted. (brighthub.com)
- The hemoglobin A1c test is also called 'glycosylated hemoglobin' test or 'glycated hemoglobin' test. (howstuffworks.com)
- We test each donor's hemoglobin at our donations centres and we require a minimum of 120 g/L (females) and 125g/L (male) to be eligible to donate at the time of your appointment. (blood.ca)
- I am a healthy female donor, but I seem to fail my hemoglobin test every second time. (blood.ca)
- What is the Hemoglobin A1C Test? (wisegeek.com)
- This forms glycated hemoglobin , which is detected by a hemoglobin A1c laboratory test. (wisegeek.com)
- There are certain individuals for whom the hemoglobin A1c test is not recommended. (wisegeek.com)
- The quantity of Hemoglobin in the test sample can be interpolated from the standard curve constructed from the standards, and corrected for sample dilution. (abcam.com)
Concentrations1
- Geometric mean and selected percentiles of hemoglobin adduct concentrations (in pmol/g hemoglobin) for the non-smoking population* from the National Health and Nutrition Examination Survey. (cdc.gov)
Search1
- Your search returned 94 Hemoglobin mu ELISA ELISA Kit across 9 suppliers. (biocompare.com)
Claim 1 wherein7
- 10. The apparatus according to claim 1 wherein said hemoglobin content of said blood sample can vary between 4 to 24 g/dl of said blood sample volume. (google.ca)
- 2. The pharmaceutical composition of claim 1 wherein the hemoglobin is reduced gastrointestinal effect hemoglobin, low gastrointestinal effect hemoglobin, low pressor effect hemoglobin, or hemoglobin which exhibits decreased aggregate formation when stored in solution in deoxygenated form for prolonged periods. (freepatentsonline.com)
- 2. The composition of claim 1 wherein the partially deoxygenated hemoglobin solution contains less than 1000 parts per million of oxygen. (google.com.au)
- 7. The composition of claim 1 wherein the reducing agent is less than 3 moles of reducing agent per mole of hemoglobin. (google.com.au)
- 9. The composition of claim 1 wherein the storage stable hemoglobin is storage stable for at least one year. (google.com.au)
- 10. The composition of claim 1 wherein the storage stable hemoglobin is storage stable for at least six months. (google.com.au)
- 12. The composition of claim 1 wherein the storage stable hemoglobin is storage stable up to 40 C. (google.com.au)
Definition2
- In children, the definition of a high hemoglobin count varies with age and sex. (mayoclinic.org)
- The definition of hemoglobin is the red iron pigment that makes red blood cells red. (yourdictionary.com)
High-affinity1
- Hemoglobin (Hb) Sherwood Forest is a rare high-affinity hemoglobin first described in 1977, arising from an Arg to Thr substitution at codon 104 of the beta chain. (hindawi.com)
Carbon dioxide3
- Hemoglobin is involved in the transport of other gases: It carries some of the body's respiratory carbon dioxide (about 20-25% of the total ) as carbaminohemoglobin , in which CO 2 is bound to the heme protein. (wikipedia.org)
- Red blood cells have no nucleus, because most of their bulk is made up of hemoglobin, a compound that carries gases, such as oxygen and carbon dioxide. (reference.com)
- Hemoglobin is not only an oxygen binding protein, it plays a key role in the respiratory pathway which includes binding to carbon dioxide once oxygen is released. (kenyon.edu)