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Research Article Free access | 10.1172/JCI106200

Hemoglobin Yoshizuka (G10(108)β asparagine→aspartic acid): a new variant with a reduced oxygen affinity from a Japanese family

Takashi Imamura, Shigeru Fujita, Yoshiro Ohta, Motosuke Hanada, and Toshiyuki Yanase

First Department of Medicine, Faculty of Medicine, Kyushu University, Fukuoka, Japan

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First Department of Medicine, Faculty of Medicine, Kyushu University, Fukuoka, Japan

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First Department of Medicine, Faculty of Medicine, Kyushu University, Fukuoka, Japan

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First Department of Medicine, Faculty of Medicine, Kyushu University, Fukuoka, Japan

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First Department of Medicine, Faculty of Medicine, Kyushu University, Fukuoka, Japan

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Published December 1, 1969 - More info

Published in Volume 48, Issue 12 on December 1, 1969
J Clin Invest. 1969;48(12):2341–2348. https://doi.org/10.1172/JCI106200.
© 1969 The American Society for Clinical Investigation
Published December 1, 1969 - Version history
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Abstract

During the course of a survey, a new hemoglobin, designated hemoglobin Yoshizuka, has been encountered in a Japanese family. Clinically, mild anemia was noted in five of six heterozygous individuals but no other significant abnormalities were found. Hemoglobin Yoshizuka is characterized by the substitution of aspartic acid for asparagine at the tenth residue of the G helix in the β-chain. Reduced oxygen affinity with almost normal heme-heme interaction was found to be a property of this abnormal hemoglobin.

The asparagine residue G10(108)β lies in the internal cavity of the tetrameric molecule and its main chain carbonyl is thought to be hydrogen bonded to histidine G10(103)α at the region of contact between α- and β-chains. It would appear likely that the introduction of a carboxyl group into the central cavity might result in interactions between the polar groups and the substituted side chain, disrupting the system of hydrogen bonds which contribute to the stability of the contacts between unlike subunits.

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