Hemoglobin by molecules such as carbon monoxide (for example, from tobacco smoking, exhaust gas, and incomplete combustion in furnaces). CO competes with oxygen at the heme binding site. Hemoglobin's binding affinity for CO is 250 times greater than its affinity for oxygen, meaning that small amounts of CO dramatically reduce hemoglobin's ability to transport oxygen. Since carbon monoxide is a colorless, odorless and tasteless gas, and poses a potentially fatal threat, carbon monoxide detectors have become commercially available to warn of dangerous levels in residences. When hemoglobin combines with CO, it forms a very bright red compound called carboxyhemoglobin, which may
Hemoglobin variants conditions that involve the red blood cells. Elevated Hemoglobin F levels are also associated with Leukemia and myeloproliferative disorders. Hemoglobin H increases the affinity for oxygen. This means that it holds onto the oxygen instead of releasing it into tissue and cells. Hb H usually occurs in some alpha thalassemia and is composed of four beta globin (protein) chains. This variant is usually produced in response to a severe shortage of alpha chains, and usually cause beta chains to function abnormally. Hemoglobin variants Hemoglobin variants are mutant forms of hemoglobin in a population (usually of humans), caused by variations in