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 (HbO
2) transports oxygen from the lungs to the tissues where the oxygen is readily released and HbO
2 becomes Hb. When Hb is exposed to certain chemicals, its normal respiratory function is blocked; thus, oxygen in HbO
2 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.