haemoglobin


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haemoglobin

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.

haemoglobin

the iron-containing protein with the property of binding oxygen, contained in red blood cells. See also oxyhaemoglobin dissociation curve.

haemoglobin

; Hb red-coloured protein within erythrocytes (6% haem; 94% globin); transports oxygen (as oxyhaemoglobin) from lungs to tissues, where oxygen is readily given up and oxyhaemoglobin is reduced to haemoglobin (see glycosylated haemoglobin)

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 ?
Extraction and purification processes produce a sterile, pyrogen-free solution containing glutaraldehyde cross-linked bovine haemoglobin polymers, with an average molecular weight of 250 kD, in a balanced salt solution.
This haemoglobin polymer has an oxygen dissociation curve that is right-shifted with a P50 of 43 mmHg, compared with 27 mmHg for human haemoglobin.
Bovine-derived haemoglobin solution (HBOC-201) was first registered for routine clinical use in South Africa for the treatment of adult surgical anaemia.
Haemoglobin Hammersmith (beta-42 (CDI) Phe replaced by Ser).
Haemoglobin M Saskatoon with slight constant haemolysis, markedly increased by sulphonamides.
Variant Haemoglobins has four introductory chapters followed by an invaluable atlas.
common haemoglobins of major clinical or diagnostic importance
Haemoglobin is contained within red blood cells and is essential for transporting oxygen around the body.
Problems with haemoglobin production cause common diseases, such as anaemia, which comes from low levels of haemoglobin and is found in 25 percent of the world's population.
If your treatment changes, or if your blood-sugar level stays too high, you should get a haemoglobin A1c test at least every three months until your blood-sugar level improves.
For example, if your levels weren't in control three weeks ago, glycated haemoglobin will persist in the blood cells that were active at that time.
An inexpensive and reliable new haemoglobin colour scale for assessing anaemia.