Hemoglobin Okaloosa (β48 (CD7) Leucine → Arginine). AN UNSTABLE VARIANT WITH LOW OXYGEN AFFINITY

S. Charache; B. Brimhall; P. Milner

doi:10.1172/JCI107482

^{Department of Medicine, Johns Hopkins Medical School and Johns Hopkins Hospital, Baltimore, Maryland 21205}

^{Department of Biochemistry, University of Oregon Medical School, Portland, Oregon 97201}

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^{Department of Medicine, Johns Hopkins Medical School and Johns Hopkins Hospital, Baltimore, Maryland 21205}

^{Department of Biochemistry, University of Oregon Medical School, Portland, Oregon 97201}

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

^{Department of Medicine, Johns Hopkins Medical School and Johns Hopkins Hospital, Baltimore, Maryland 21205}

^{Department of Biochemistry, University of Oregon Medical School, Portland, Oregon 97201}

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Published in Volume 52, Issue 11 on November 1, 1973
J Clin Invest. 1973;52(11):2858–2864. https://doi.org/10.1172/JCI107482.
© 1973 The American Society for Clinical Investigation

Published November 1, 1973 - Version history

A slow-moving hemoglobin with electrophoretic mobility similar to that of hemoglobin S was discovered in a white laboratory technologist. She had an elevated reticulocyte count, as did several members of her family. Her red cell survival was shortened. Amino acid analysis indicated that leucine at position β48 (CD7) had been replaced by arginine. The abnormal hemoglobin, called Okaloosa, was heat-precipitable and had decreased oxygen affinity. It exhibited a greater change in oxygen affinity than hemoglobin A when 2,3 DPG was added to “stripped” hemolysates. These findings cannot be readily explained by current views of structure-function relationships in the hemoglobin molecule. However, it is of interest that the amino acid in position CD7 is normally leucine in the α, β, δ, and γ-hemoglobin chains and in the myoglobin chain of man and a wide variety of other vertebrates.

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