Published in Volume 46, Issue 11 (November 1967)
J Clin Invest. 1967;46(11):1840–1847. doi:10.1172/JCI105674.
Copyright © 1967, The American Society for Clinical Investigation.

Articles

Hemoglobin Yakima: I. Clinical and Biochemical Studies*

Richard T. Jones, Edwin E. Osgood, Bernadine Brimhall and Robert D. Koler^‡

Department of Biochemistry and the Division of Experimental Medicine, University of Oregon Medical School, Portland, Oregon

^‡ Address requests for reprints to Dr. Robert D. Koler, Division of Experimental Medicine, University of Oregon Medical School, 3181 S. W. Sam Jackson Park Road, Portland, Oreg. 97201.

^* Submitted for publication 16 May 1967 and in revised form 26 June 1967.

Published November 1967

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.