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Concise Publication Free access | 10.1172/JCI107125

Oxygen equilibrium of hemoglobin E

H. Franklin Bunn, W. Delano Meriwether, Stanley P. Balcerzak, and Donald L. Rucknagel

Thorndike Memorial Laboratory, Harvard Medical Service, Boston City Hospital, Boston 02118

Harvard Medical School, Boston, Massachusetts 02115

Department of Medicine, Ohio State University, Columbus, Ohio 43210

Department of Human Genetics, University of Michigan School of Medicine, Ann Arbor, Michigan 48105

Find articles by Bunn, H. in: PubMed | Google Scholar

Thorndike Memorial Laboratory, Harvard Medical Service, Boston City Hospital, Boston 02118

Harvard Medical School, Boston, Massachusetts 02115

Department of Medicine, Ohio State University, Columbus, Ohio 43210

Department of Human Genetics, University of Michigan School of Medicine, Ann Arbor, Michigan 48105

Find articles by Meriwether, W. in: PubMed | Google Scholar

Thorndike Memorial Laboratory, Harvard Medical Service, Boston City Hospital, Boston 02118

Harvard Medical School, Boston, Massachusetts 02115

Department of Medicine, Ohio State University, Columbus, Ohio 43210

Department of Human Genetics, University of Michigan School of Medicine, Ann Arbor, Michigan 48105

Find articles by Balcerzak, S. in: PubMed | Google Scholar

Thorndike Memorial Laboratory, Harvard Medical Service, Boston City Hospital, Boston 02118

Harvard Medical School, Boston, Massachusetts 02115

Department of Medicine, Ohio State University, Columbus, Ohio 43210

Department of Human Genetics, University of Michigan School of Medicine, Ann Arbor, Michigan 48105

Find articles by Rucknagel, D. in: PubMed | Google Scholar

Published November 1, 1972 - More info

Published in Volume 51, Issue 11 on November 1, 1972
J Clin Invest. 1972;51(11):2984–2987. https://doi.org/10.1172/JCI107125.
© 1972 The American Society for Clinical Investigation
Published November 1, 1972 - Version history
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Abstract

Oxygen equilibrium was determined on hemoglobin of individuals both heterozygous and homozygous for hemoglobin E. The whole blood oxyhemoglobin dissociation curve of AE blood was identical to that of normal AA blood. E hemoglobin, isolated by diethylaminoethyl Sephadex and carboxymethyl cellulose column chromatography, had oxygen affinity, heme-heme interaction, and Bohr effect identical to those of hemoglobin A prepared from the same column. Furthermore, the two hemoglobins had equal reactivity with 2,3-diphosphoglycerate. Phosphate-free hemolysates of blood from E and A homozygotes also had identical oxygen saturation curves. These results do not confirm earlier reports that hemoglobin E has an abnormally low oxygen affinity.

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