Hemoglobin the iron gets recycled. This process also produces one molecule of carbon monoxide for every molecule of heme degraded. Heme degradation is one of the few natural sources of carbon monoxide in the human body, and is responsible for the normal blood levels of carbon monoxide even in people breathing pure air. The other major final product of heme degradation is bilirubin. Increased levels of this chemical are detected in the blood if red blood cells are being destroyed more rapidly than usual. Improperly degraded hemoglobin protein or hemoglobin that has been released from the blood cells too rapidly can
Embryonic hemoglobin two beta chains. It is quite unstable, more so than even hemoglobin Gower 1, and breaks down very rapidly under stress. Despite this, it has been proposed as a candidate for reactivation in cases of severe α thalassemia or hemoglobinopathies afflicting the alpha chain. Embryonic hemoglobin The human embryonic haemoglobins were discovered in 1961. These were Hb-Gower 1, consisting of 2 zeta chains and 2 epsilon chains, and Hb-Gower 2, which consists of 2 αlpha-chains and 2 epsilon-chains, the zeta and epsilon chains being the embryonic haemoglobin chains. Embryonic hemoglobin is a tetramer produced in the blood islands in the