| GHb | Glycated haemoglobin |
|---|---|
| Hgb | Haemoglobin |
| Hb A1 | Haemoglobin A1 |
| Hb C | Haemoglobin C |
| Hb F | Haemoglobin F |
| haemoglobin | <cell biology, haematology> Four subunit globular oxygen carrying protein of the erythrocytes of vertebrates and some invertebrates. It is a conjugated protein containing four haem groups and globin. There are two alpha and two beta chains (very similar to myoglobin) in adult humans, the haem moiety (an iron containing substituted porphyrin) is firmly held in a nonpolar crevice in each peptide chain. There are four globin polypeptide chains, designated alpha, beta, gamma, delta in the adult. Each is composed of several hundred amino acids. (08 Mar 2000) |
|---|---|
| haemoglobin A | <haematology> Haemoglobin A is the normal form of the protein haemoglobin which is found in adults. It is composed of two alpha chains and two beta chains. (09 Oct 1997) |
| haemoglobin a, glycosylated | Minor haemoglobin components of human erythrocytes designated a1a, a1b, and a1c. Haemoglobin 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 haemoglobin a is a more reliable index of the blood sugar average over a long period of time. (12 Dec 1998) |
| haemoglobin A1C | <haematology> The substance of red blood cells that carries oxygen to the cells and sometimes joins with glucose. Because the glucose stays attached for the life of the cell (about 4 months), a test to measure haemoglobin A1C shows what the person's average blood glucose level was for that period of time. (09 Oct 1997) |
| haemoglobin A2 | <chemical> An adult haemoglobin component normally present in haemolysates from human erythrocytes in concentrations of about 3%. The haemoglobin is composed of two alpha chains and two delta chains. The percentage of hba2 varies in some haematologic disorders, but is about double in beta-thalassaemia. Chemical name: Haemoglobin A2 (12 Dec 1998) |
| haemoglobin AIc | The major fraction of glycosylated haemoglobin. (05 Mar 2000) |
| haemoglobin Anti-Lepore | A group of abnormal haemoglobins similar to haemoglobin Lepore. These haemoglobins have normal a chains, but the non-a chain consists of the N-terminal portion of the b chain joined to the C-terminal portion of the d chain. This is the opposite crossing over pattern observed in haemoglobin Lepore. Examples of haemoglobin Anti-Lepore include HbMiyada, Hb PCongo, Hb PNilotic, and HbLincoln Park. There is also one variant that is both haemoglobin Lepore and haemoglobin Anti-Lepore (HbParchman). Compare: haemoglobin Lepore. (05 Mar 2000) |
| haemoglobin Bart's | A Hb homotetramer (all four polypeptides identical) of formula g4, found in the early embryo and in alpha-thalassaemia 2; not effective in oxygen transport; does not display a Bohr effect. (05 Mar 2000) |
| haemoglobin C | <haematology> Haemoglobin C is an abnormal version of the protein haemoglobin. The sixth amino acid of the normal beta chain, glutamic acid, is replaced by lysine in haemoglobin C. This mutation causes the red blood cell to be less flexible. (09 Oct 1997) |
| haemoglobin C disease | <haematology> A rare genetic disease of the haemoglobin. Patients are anemic due to the premature breakdown of the blood cells in the spleen. Jaundice may be seen in some patients. There is no specific treatment other than supportive care. (27 Sep 1997) |
| haemoglobin Chesapeake | An abnormal Hb with a single a chain substitution, molecular formula a292Arg→Leub2A; heterozygotes have polycythemia, apparently to compensate for the increased oxygen affinity of this Hb, resulting in decreased liberation of oxygen in the tissues. (05 Mar 2000) |
| haemoglobin Constant Spring | An abnormal haemoglobin having an extended polypeptide chain (31 additional amino acid residues) on the a chain (thus, the a chain is 172 amino acids long); approximately 20% of the individuals with Hb H disease also have this defect. (05 Mar 2000) |
| haemoglobin DPunjab | An abnormal Hb with a single b chain substitution, molecular formula a2Ab2121Glu→ Gln; heterozygotes are asymptomatic, homozygotes have mild haemolytic anaemia; there is an increase in O2 affinity; identical to haemoglobin DLos Angeles, haemoglobin DNorth Carolina, haemoglobin DPortugal, haemoglobin DChicago, and haemoblogin Oak Ridge. (05 Mar 2000) |
| haemoglobin E | <haematology> Haemoglobin E is an abnormal version of the protein haemoglobin, found in Southeast Asia, which plays a role in such medical conditions as microcythaemia, target cell formation, and mild haemolytic anaemia. The beta chain of the haemoglobin is altered because of a mutation. (09 Oct 1997) |
| haemoglobin electrophoresis | <investigation> A special diagnostic procedure which identifies abnormal haemoglobin proteins by the way they migrate in an electric field (electrophoresis). The electric field is used to separate haemoglobin proteins from each other and allow the identification of different components. This can be used to diagnose thalassaemia, sickle cell disease and haemoglobin C disease. (18 Nov 1997) |
| aberrant haemoglobin | A mutant Hb that functions abnormally. Compare: variant haemoglobin. (05 Mar 2000) |
|---|---|
| bile pigment haemoglobin | <protein> A protein which is formed from the breakdown of haemoglobin (a protein that carries oxygen in the blood) and is a precursor to the bile pigment biliverdin. (09 Oct 1997) |
| carbon monoxide haemoglobin | <chemical> Chemical name: Haemoglobins, carbonyl- (12 Dec 1998) |
| variant haemoglobin | A harmless mutant form of Hb. (05 Mar 2000) |
| reduced haemoglobin | The form of Hb in red blood cells after the oxygen of oxyhemoglobin is released in the tissues. (05 Mar 2000) |
| mean corpuscular haemoglobin | The haemoglobin content of the average red cell, calculated from the haemoglobin therein and the red cell count, in erythrocyte indices. (05 Mar 2000) |
| mean corpuscular haemoglobin concentration | Hgb/Hct;the average haemoglobin concentration in a given volume of packed red cells, calculated from the haemoglobin therein and the haematocrit, in erythrocyte indices. (05 Mar 2000) |
| glycosylated haemoglobin | <biochemistry> A test which measures the amount of glucose-bound haemoglobin. As the blood glucose level increases the proportion of haemoglobin molecules which bind glucose increases with time. The measurement of glycosylated haemoglobin yields important information regarding how well a patients diabetes is being controlled. (27 Sep 1997) |
| glycosylated haemoglobin test | <investigation> A blood test that measures a person's average blood glucose (sugar) level for the 2- to 3-month period before the test. See: haemoglobin A1C. (09 Oct 1997) |
| green haemoglobin | <protein> A protein which is formed from the breakdown of haemoglobin (a protein that carries oxygen in the blood) and is a precursor to the bile pigment biliverdin. (09 Oct 1997) |
| muscle haemoglobin | <physiology> Protein (17.5 kD) found in red skeletal muscle. It was the first protein for which the tertiary structure was determined by X-ray diffraction, by J.C.Kendrew's group working on sperm whale myoglobin. It is a single polypeptide chain of 153 amino acids, containing a haem group bonded via its ferric iron to two histidine residues. It binds oxygen noncooperatively and has a higher affinity for oxygen than haemoglobin at all partial pressures. In capillaries oxygen is effectively removed from haemoglobin and diffuses into muscle fibres where it binds to myoglobin which acts as an oxygen store. (18 Nov 1997) |
| hereditary persistence of foetal haemoglobin | <haematology> Hereditary persistence of foetal haemoglobin is a genetic condition where adult types of haemoglobin fail to develop and the types of haemoglobin the individual had as a foetus remains present well past the point when they would normally have stopped being produced. (09 Oct 1997) |
| sickle cell haemoglobin | <haematology> Haemoglobin S is an abnormal version of the protein haemoglobin. The sixth amino acid of the normal beta chain, glutamic acid, is replaced by valine with gluconic acid. This mutation causes the red blood cell to take on a sickle shape, and is the cause of the sickle cell trait condition (when the individual is heterozygous for this mutant haemoglobin) and the disease of sickle cell anaemia (when the individual is homozygous for this mutant haemoglobin). (09 Oct 1997) |
| oxygenated haemoglobin | <physiology> See Hemoglobin. Origin: Oxy- + haemoglobin, hemoglobin. Source: Websters Dictionary (01 Mar 1998) |
| embryonic haemoglobin | See: haemoglobin Gower-1, haemoglobin Gower-2. (05 Mar 2000) |
| haemoglobin | a hemoprotein composed of globin and heme that gives red blood cells their characteristic color |
|---|---|
| haemoglobin | presence of excessive hemoglobin in the blood plasma |
| haemoglobin | a blood disease characterized by the presence of abnormal hemoglobins in the blood |
| haemoglobin | presence of hemoglobin in the urine |
제품명 |
판매사 |
보험코드 | 성분/함량 | 구분/보험급여 |
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제품명 |
판매사 |
보험코드 | 성분/함량 | 구분/보험급여 |
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