Hb Moriguchi or α₂β₂97(FG4)His→Tyr Substitution at the α₁-₋β₂ Interface

Y. Ohba Department of Clinical Laboratory Science, Yamaguchi University School of Medicine, 1144, Kogushi, Ube, 755, Japan

K. Imai Department of Physicochemical Physiology, Medical School, Osaka University, 4–3–57 Nakanoshima, Kita-ku, Osaka, 530, Japan

I. Kumada Central Laboratory Department of Internal Medicine, Matsushita Memorial Hospital, 2–35 Sotozima-cho, Moriguchi-city, Osaka, 570, Japan

A. Ohsawa Central Laboratory Department of Internal Medicine, Matsushita Memorial Hospital, 2–35 Sotozima-cho, Moriguchi-city, Osaka, 570, Japan

T. Miyaji Department of Clinical Laboratory Science, Yamaguchi University School of Medicine, 1144, Kogushi, Ube, 755, Japan

Abstract

An abnormal profile of cation exchange high performance liquid chromatography for the determination of Hb A_1c led to the discovery of a new hemoglobin variant with a His→Tyr substitution at position 97(FG4) of the β chain. The variant comprised about equal proportion to normal Hb A. Lt showed an increased oxygen affinity, normal n value and slightly reduced alkaline Bohr effect. However, the magnitude of the functional deviation is less than that of other variants with substitutions at the same position, and the heterozygous carrier was not erythremic.

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Hb Moriguchi or α₂β₂97(FG4)His→Tyr Substitution at the α₁-₋β₂ Interface

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Hb Moriguchi or α₂β₂97(FG4)His→Tyr Substitution at the α₁-₋β₂ Interface