Hemoglobin failure, or abnormal hemoglobin (such as that of sickle-cell disease). The ability of each hemoglobin molecule to carry oxygen is normally modified by altered blood pH or CO, causing an altered oxygen–hemoglobin dissociation curve. However, it can also be pathologically altered in, e.g., carbon monoxide poisoning. Decrease of hemoglobin, with or without an absolute decrease of red blood cells, leads to symptoms of anemia. Anemia has many different causes, although iron deficiency and its resultant iron deficiency anemia are the most common causes in the Western world. As absence of iron decreases heme synthesis, red blood cells in iron deficiency
Fetal hemoglobin blood cells, this substance decreases the affinity of hemoglobin for oxygen. 2,3-BPG is also present in fetal red blood cells, but interacts less efficiently with fetal hemoglobin than adult hemoglobin. This is due to a change in a single amino acid (residue 143) found in the 2,3-BPG 'binding pocket': from histidine to serine, which gives rise to the greater oxygen affinity. Whereas histidine is positively charged and interacts well with the negative charges found on the surface of 2,3-BPG, Serine has a neutrally charged side chain at physiological pH, and interacts less well. This change results in less binding of