Richard T. Jones, Edwin E. Osgood, Bernadine Brimhall, Robert D. Koler
J Clin Invest.
1967;
46(11):1840–1847
doi:10.1172/JCI105674
This article Copyright © 1967, The American Society for Clinical Investigation
Abstract
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T
hree 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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