HB Kanagawa [α40(C5)LYS→MET]: A New α Chain Variant with an Increased Oxygen Affinity

H. Miyashita First Department of Internal Medicine, Yokohama City University School of Medicine Urafune, Minami-ku, Yokohama, 232, Japan

K. Hashimoto First Department of Internal Medicine, Yokohama City University School of Medicine Urafune, Minami-ku, Yokohama, 232, Japan

H. Mohri First Department of Internal Medicine, Yokohama City University School of Medicine Urafune, Minami-ku, Yokohama, 232, Japan

T. Ohokubo First Department of Internal Medicine, Yokohama City University School of Medicine Urafune, Minami-ku, Yokohama, 232, Japan

T. Harano Department of Biochemistry, Kawasaki Medical School, Kurashiki, Okayama, 701-01, Japan

K. Harano Department of Biochemistry, Kawasaki Medical School, Kurashiki, Okayama, 701-01, Japan

K. Imai Department of Physicochemical, Physiology Osaka University Medical School Nakamoshima, Fukushima-ku, Osaka, 553, Japan

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Abstract

An abnormal hemoglobin was suspected in a 70-year-old Japanese male with cerebral infarction and erythremia with high performance liquid chromatography assay of Hb A_1c. The hemoglobin variant migrated to the anode more rapidly than Hb A. Structure determination studies, including amino acid analysis of the abnormal pep-tide and DNA sequencing of a partially cloned α-globin gene, demonstrated that it is a new hemoglobin variant which has been named Hb Kanagawa [α40(C5)Lys→Met]. This variant showed an increased oxygen affinity, decreased heme-heme interaction, and a lowered 2,3-diphosphoglycerate effect relative to normal.

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HB Kanagawa [α40(C5)LYS→MET]: A New α Chain Variant with an Increased Oxygen Affinity

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HB Kanagawa [α40(C5)LYS→MET]: A New α Chain Variant with an Increased Oxygen Affinity

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