Hemoglobin. 1978;2(1):85-8.

The structure of hemoglobin Hopkins-2.

Abstract

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.

PMID:: 646867; [PubMed - indexed for MEDLINE]

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Hemoglobin-Strumica or alpha 2 112(G19) His replaced by Arg beta 2. (With an addendum: hemoglobin-J-Paris-I, alpha 2 12(A10) Ala replaced by Asp beta 2, in the same population). [Biochim Biophys Acta. 1975]
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Jones RT, Brimhall B, Pootrakul S, Gray G. J Mol Evol. 1976 Dec 31; 9(1):37-44.

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