HB Mtyano or α41(C6)Thr→Ser: A new High Oxygen Affinity α Chain Variant Found in an Erythremic Blood Donor

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

R. Uenaka Department of Physicochemical, Physiology Medical School Osaka University, 4-3-57 Nakanoshima, Kita-ku, Osaka, 530, Japan

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

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

K. Itoh Red Cross Blood Center, Yamaguchi Prefecture, 172, Noda, Yamaguchi, Japan

K. Hirakawa Red Cross Blood Center, Yamaguchi Prefecture, 172, Noda, Yamaguchi, Japan

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

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Abstract

An abnormal hemoglobin found in an erythremic blood donor was separable only by isoelectrofocusing, where it was located at the cathodic edge of Hb A. Cation exchange high performance liquid chromatography of a tryptic digest from the total a chain revealed splitting of the αT-6 peak, although our routine procedures failed to uncover the abnormality. This enabled the chemical characterization and quantitation of the abnormal hemoglobin as α41 (C6)Thr→Ser comprising about 30% of the total hemoglobin. The purified hemoglobin showed increased oxygen affinity, decreased subunit cooperativity and effect of organic phosphates, and normal Bohr effect.

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HB Mtyano or α41(C6)Thr→Ser: A new High Oxygen Affinity α Chain Variant Found in an Erythremic Blood Donor

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HB Mtyano or α41(C6)Thr→Ser: A new High Oxygen Affinity α Chain Variant Found in an Erythremic Blood Donor

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