Hemoglobin Yakima: I. Clinical and Biochemical Studies*
Open Access
- 1 November 1967
- journal article
- research article
- Published by American Society for Clinical Investigation in JCI Insight
- Vol. 46 (11), 1840-1847
- https://doi.org/10.1172/jci105674
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.This publication has 19 references indexed in Scilit:
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