Transformation of Hemoglobin by Various Peroxides in Vitro
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概要
- 論文の詳細を見る
Hydrogen peroxide converted HbO_2 and DeoxyHb into MetHb, and MetHb into the complex [MetHbOOH], which readily regenerated MetHb. tert-Butyl hydroperoxide converted HbO_2 and DeoxyHb into MetHb, and MetHb into a complex which was rather stable. The formation of MetHb was mainly due to the direct action of each of these peroxides, and was influenced by the allosteric effector, IHP. Ascorbic acid affected the hydrogen peroxide-induced MetHb formation, probably due to hydroxyl radical produced during the interaction of ascorbic acid with hydrogen peroxide. HbO_2 and DeoxyHb treated with linoleic acid hydroperoxide at pH 7-8 produced MetHb in the presence of albumin or KCN. Complex formation between MetHb and linoleic acid hydroperoxide occurred at pH 8,and it was prevented by albumin and KCN. The reaction of MetHb with the hydroperoxide at pH 7 produced precipitates, and that at pH 7.4 yielded the complex and then precipitates. It was suggested that the interaction of MetHb with hydroperoxide first produced the complex, which regenerated MetHb with the production of some active species for cross-linking of hemoglobin tetramer upon treatment at a lower pH value or in the presence of albumin.
- 公益社団法人日本薬学会の論文
- 1983-01-25
著者
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菊川 清見
Tokyo College of Pharmacy
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呉地 伝夫
Tokyo College of Pharmacy
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呉地 伝夫
東京薬科大学
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笹原 富弥
Tokyo College of Pharmacy
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