Hemoglobin Hopkins-2
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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. The specific mutation in Hemoglobin Hopkins-2 results in two abnormal α chains (human hemoglobin consist of 2 α and 2 β polypeptides usually termed chains).[1] The mutation is the result of histidine 112 being replaced with aspartic acid in the protein's polypeptide sequence.[1] Additionally, within one of the mutated alpha chains, there are substitutes at 114 and 118, two points on the amino acid chain.[2] This mutation can cause sickle cell anemia.[3]
Following the initial discovery of hemoglobin, two researchers working at Johns Hopkins Hospital in the mid-twentieth century, Ernest W. Smith and J.V. Torbert, discovered the Hopkins-2 mutation of hemoglobin.[4] Work by Harvey A. Itano and Elizabeth A. Robinson in 1960 confirmed Smith's and Torbert's finding and emphasized the importance of the alpha loci in the mutation.[5] Later in the twentieth century, Samuel Charache, another Hopkins affiliated scientist and doctor, studied the physiological impacts of the variant on health.[6] His findings suggest that the variant plays no effect clinically.[7]