| GHb | Glycated haemoglobin |
|---|---|
| Hgb | Haemoglobin |
| Hb A1 | Haemoglobin A1 |
| Hb C | Haemoglobin C |
| Hb F | Haemoglobin F |
| Lepore haemoglobin | <haematology> Variant haemoglobin in a rare form of thalassaemia: there is a composite _ _ chain as a result of an unequal crossing over event. The composite chain is functional but synthesised at reduced rate. (18 Nov 1997) |
|---|
| 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 Lepore | A group of abnormal Hb's with normal a chains, but the non-a chains consist of the N-terminal portion of the d chain joined to the C-terminal portion of the b chain, apparently as the result of nonhomologous pairing and crossing over between the genes for b and d chains. The major types are Hb LeporeBoston (identical to Hb LeporeWashington), Hb LeporeHollandia, and Hb LeporeBaltimore, which differ in the region of crossing over (d87-b116, d22-b50, and d50-b86, respectively). Heterozygotes form about 10% Hb Lepore, normal amounts of Hb A2, and moderately increased amounts of Hb F and usually have mild anaemia, microcytosis, and hypochromia; homozygotes form only Hb Lepore and Hb F and have severe anaemia. Compare: haemoglobin Anti-Lepore. (05 Mar 2000) |
| Lepore thalassaemia | Thalassaemia syndrome due to production of abnormally structured Lepore haemoglobin. Heterozygous state: thalassaemia minor with about 10% of Hb Lepore, Hb F moderately increased, Hb A2 normal. Homozygous state: thalassaemia major with only Hb F and Hb Lepore produced, no Hb A or Hb A2. (05 Mar 2000) |
| 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) |
| 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) |
제품명 |
판매사 |
보험코드 | 성분/함량 | 구분/보험급여 |
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제품명 |
판매사 |
보험코드 | 성분/함량 | 구분/보험급여 |
|---|