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 such as pure water, alcohol or ether, followed by slow evaporation of the solvent from the resulting protein solution. Hemoglobin's reversible oxygenation was described a few years later by Felix Hoppe-Seyler. In 1959, Max Perutz determined the molecular structure of hemoglobin by X-ray crystallography. This work resulted in his sharing with John Kendrew the 1962 Nobel Prize in Chemistry for their studies of the structures of globular proteins. The role of hemoglobin in the blood was elucidated by French physiologist Claude Bernard. The name "hemoglobin" is derived from the words "heme" and "globin", reflecting the fact that each subunit of