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. 1967 Nov;46(11):1840–1847. doi: 10.1172/JCI105674

Hemoglobin Yakima: I. Clinical and Biochemical Studies*

Richard T Jones 1, Edwin E Osgood 1, Bernadine Brimhall 1, Robert D Koler 1,‡
PMCID: PMC292934  PMID: 6061751

Abstract

Three members of a family who have erythrocytosis and a new hemoglobin, designated hemoglobin Yakima, are described.

The abnormal hemoglobin is characterized by the substitution of histidine for aspartic acid at residue 99 in the β-chain.

Of three possible structure-function relations which would account for the increased oxygen affinity of hemoglobin Yakima, only two seem likely. These are: (a) an intrachain shift in the normal relations between the F and G helices and the heme group, or (b) an effect of the substituted side chain at a region of contact between nonpolar residues of the α- and β-chains which favors the oxyhemoglobin quarternary structure.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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