| HPAFT | hereditary persistence of alfa-fetoprotein |
|---|---|
| HPFH | hereditary persistence of fetal hemoglobin |
| N-P | need-persistence |
| AHC | Albright's Hereditary Osteodystrophy |
| AHO | Albright's Hereditary Osteodystrophy |
| HPFH | Hereditary Persistence of Fetal Hemoglobin |
|---|---|
| FHR | Foetal heart rate |
| IUGR | Intrauterine foetal growth retardation |
| GHb | Glycated haemoglobin |
| Hgb | Haemoglobin |
| 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) |
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| persistence | 1. The tendency of a cell to continue moving in one direction: an internal bias on the random walk behaviour that cells exhibit in isotropic environments. 2. Of viruses that persist in a cell population, animal, plant or population for long periods often in a nonreplicating form, by such strategies as integration into host DNA, immunological suppression or mutation into forms with slow replication. (18 Nov 1997) |
|---|---|
| foetal haemoglobin | <chemical> The form of haemoglobin normally comprising more than half of the haemoglobin in the foetus, composed of two alpha and two gamma polypeptides. It is also present in minimal amounts in adulthood and is abnormally elevated in aplastic anaemia, leukaemia, and certain types of thalassaemia. It has higher affinity for oxygen under physiologic conditions than does haemoglobin a. Chemical name: Haemoglobin F (12 Dec 1998) |
| 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) |
| 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) |
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