Hemoglobin Yakima: I. Clinical and Biochemical Studies

Richard T. Jones; Edwin E. Osgood; Bernadine Brimhall; Robert D. Koler

doi:10.1172/JCI105674

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.

Presented in part at the Twentieth Annual Meeting of the Western Society for Clinical Research, 26 January 1967, at Carmel, Calif.

This investigation was supported in part by U. S. Public Health Service grant CA-07941 and by the U. S. Atomic Energy Commission (RLO-581-14).

Find articles by Jones, R. in: PubMed | Google Scholar

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.

Presented in part at the Twentieth Annual Meeting of the Western Society for Clinical Research, 26 January 1967, at Carmel, Calif.

This investigation was supported in part by U. S. Public Health Service grant CA-07941 and by the U. S. Atomic Energy Commission (RLO-581-14).

Find articles by Osgood, E. in: PubMed | Google Scholar

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.

Presented in part at the Twentieth Annual Meeting of the Western Society for Clinical Research, 26 January 1967, at Carmel, Calif.

This investigation was supported in part by U. S. Public Health Service grant CA-07941 and by the U. S. Atomic Energy Commission (RLO-581-14).

Find articles by Brimhall, B. in: PubMed | Google Scholar

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.

Presented in part at the Twentieth Annual Meeting of the Western Society for Clinical Research, 26 January 1967, at Carmel, Calif.

This investigation was supported in part by U. S. Public Health Service grant CA-07941 and by the U. S. Atomic Energy Commission (RLO-581-14).

Find articles by Koler, R. in: PubMed | Google Scholar

Published in Volume 46, Issue 11 on November 1, 1967
J Clin Invest. 1967;46(11):1840–1847. https://doi.org/10.1172/JCI105674.
© 1967 The American Society for Clinical Investigation

Published November 1, 1967 - Version history

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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