The structure of hemoglobin Hopkins-2.
Hemoglobin Hopkins-2 was originally reported to contain two abnormal alpha chains. Both had aspartic acid instead of the normal histidine at position alpha 112; the second alpha chain also contained two additional amino acid substitutions. In subsequent reports of the structure of this hemoglobin, only the His replaced by Asp substitution was found. To determine whether the second abnormal alpha chain was limited to the original kindred, the structure of their hemoglobin was redetermined. Only the His replaced by Asp substitution was present.
D001224:Aspartic Acid; D005260:Female; D006455:Hemoglobins, Abnormal; D006639:Histidine; D006801:Humans; D008297:Male; D008396:Maryland
D006455:Hemoglobins, Abnormal; D001224:Aspartic Acid; D006639:Histidine