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Hb Miyano or alpha 41(C6)Thr----Ser: a new high oxygen affinity alpha chain variant found in an erythremic blood donor. 1989
Y Ohba, and
K Imai, and
R Uenaka, and
M Ami, and
K Fujisawa, and
K Itoh, and
K Hirakawa, and
T Miyaji
Department of Clinical Laboratory Science, Yamaguchi University School of Medicine, Ube, Japan.
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 alpha chain revealed splitting of the alpha T-6 peak, although our routine procedures failed to uncover the abnormality. This enabled the chemical characterization and quantitation of the abnormal hemoglobin as alpha 41(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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