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
Hemoglobin Hopkins-2 Hemoglobin Hopkins-2 Hemoglobin Hopkins-2 (Hb Hop-2) is a mutation of the protein hemoglobin, which is responsible for the transportation of oxygen through the blood from the lungs to the musculature of the body in vertebrates. Generally, the mutation causes two abnormal α chains in the protein's structure. Within the chains, the mutation is the result of hemoglobin's histidine amino acid being replaced with aspartic acid in the protein's genetic sequence. This amino acid structure change occurs at residue 112. Additionally, within one of the mutated alpha chains, there are substitutes at 114 and 118, two points on the amino acid