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 Hopkins-2 that causes sickle cell, which is a disorder in which red blood cells break down and become abnormally shaped. Hemoglobin S has two beta chains, whereas hemoglobin Hopkins-2 has two alpha chains. Hopkins-2 makes up 22% of hemolysates in single heterozygotes; therefore, there is the normal version of the gene in these patients. Hemolysates are the products of the destruction of red blood cells. Ho-2 also comprises 11% of hemolysates in ‘double’ heterozygotes, which are when the gene contains both Hopkins-2 and Hemoglobin S. There are currently multiple possible explanations as to how the Hemoglobin variant Hopkins-2 works. One explanation