haemoglobin


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he·mo·glo·bin

(Hgb, Hb) (hē'mō-glō'bin)
The red respiratory protein of erythrocytes, consisting of approximately 3.8% heme and 96.2% globin, with a molecular weight of 64,450, which as oxyhemoglobin (HbO2) transports oxygen from the lungs to the tissues where the oxygen is readily released and HbO2 becomes Hb. When Hb is exposed to certain chemicals, its normal respiratory function is blocked; thus, oxygen in HbO2 is easily displaced by carbon monoxide, a process that results in the formation of fairly stable carboxyhemoglobin (HbCO), as in asphyxiation resulting from inhalation of exhaust fumes from gasoline engines. When the iron in Hb is oxidized from the ferrous to ferric state, as in poisoning with nitrates and certain other chemicals, a nonrespiratory compound, methemoglobin (MetHb), is formed.
Synonym(s): haemoglobin.

haemoglobin

The iron-containing protein that fills red blood cells. Haemoglobin combines readily but loosely with oxygen in conditions of high oxygen concentration, as in the lungs, and releases it when in an environment low in oxygen, as in the body tissues. In health, each 100 ml of blood contains 12–18 g of haemoglobin. The various genetically induced abnormalities of haemoglobin are called HAEMOGLOBINOPATHIES.

haemoglobin

a large PROTEIN molecule with a quaternary structure of four POLYPEPTIDES CHAINS, two alpha and two beta chains, each of which is complexed to a separate HAEM group. About 300 million molecules of haemoglobin occur in each red blood cell of the mammalian circulation, with each molecule binding to a maximum of four oxygen molecules, one per haem group (= oxygenation). See OXYGEN-DISSOCIATION CURVE for an explanation of oxygen carriage. Haemoglobin is found in all vertebrates and many invertebrates. In mammals the foetal haemoglobin (HbF) has a different polypeptide combination from that in postnatal ‘adult’ haemoglobin (HbA), consisting of two alpha and two gamma chains, with different oxygen-carrying characteristics (up to 30% more at low oxygen tension). An altered beta chain in HbA produces SICKLE-CELL ANAEMIA.

he·mo·glo·bin

(Hb) (hē'mō-glō'bin) [MIM*141800142310, MIM*141800]
Red respiratory protein of erythrocytes. In humans, there are at least five kinds of normal Hb: two embryonic Hbs (Hb Gower-1, Hb Gower-2), fetal (Hb F), and two adult types (Hb A, Hb A2).
Synonym(s): haemoglobin.

Patient discussion about haemoglobin

Q. haemoglobin deficiency Haemoglobin deficiency - 6.3 rbc count less than normal range. platelets are 157000

A. what you describe here is pretty harsh numbers. very very low hemoglobin, low platelets level...have you checked for white blood cells? i recommend seeing a Dr. ASAP. with these numbers there is a good chance that you'll bleed from places that are not supposed to bleed.

More discussions about haemoglobin
References in periodicals archive ?
Complete Blood count remained unremarkable except haemoglobin of 9.3 gm/dl with MCV of 77.9 fl.
KHA-CARI guideline: Biochemical and haematological targets: Haemoglobin concentration in patients using erythropoietin-stimulating agents.
HbA1c is a reaction product of glucose and the Nterminal valine of the beta chain of haemoglobin. The reaction is irreversible and enzyme independent.
The use of automated HPLC to detect and quantitate haemoglobins. Clin Lab Haematol 1997;19:171-6.
In primary THR and primary TKR, preoperative haemoglobin <130 g/l has been shown to increase the risk of transfusion by 1.5 times compared with haemoglobin 130 to 150 g/l2.
New research shows that the "vampire" bug favours human haemoglobin over that of other animals.
HBOC-201 (Hemopure) is a cell-free, polymerised haemoglobin solution that, when infused intravenously, has the following physiological and pharmacological actions:
Unexplained variability of glycated haemoglobin in nondiabetic subjects not related to glycaemia.
Now, a recent paper in The Lancet suggests that assiduous targeting of higher haemoglobin levels in anaemic patients with chronic kidney disease may also cause adverse events.