人类红细胞中谷胱甘肽代谢的酶学研究。
Studies in the enzymology of glutathione metabolism in human erythrocytes.
作者信息
Jackson R C
出版信息
Biochem J. 1969 Feb;111(3):309-15. doi: 10.1042/bj1110309.
Abstract
Spectrophotometric assay methods are described for glutathione synthetase, gamma-glutamylcysteine synthetase and gamma-glutamyl transpeptidase of erythrocytes. The contents of these enzymes in normal human erythrocytes are reported. Erythrocyte glutathione synthetase is inhibited by ADP; this inhibition is competitive with respect to ATP. gamma-Glutamylcysteine synthetase is subject to feedback inhibition by GSH, and is also inhibited by NADH, and to a lesser extent by NAD(+) and NADPH. This enzyme is irreversibly inactivated by cysteamine.
摘要
本文描述了用于检测红细胞中谷胱甘肽合成酶、γ-谷氨酰半胱氨酸合成酶和γ-谷氨酰转肽酶的分光光度测定方法。报告了这些酶在正常人红细胞中的含量。红细胞谷胱甘肽合成酶受ADP抑制；这种抑制作用对ATP而言是竞争性的。γ-谷氨酰半胱氨酸合成酶受到GSH的反馈抑制，也受到NADH的抑制，并且在较小程度上受到NAD(+)和NADPH的抑制。该酶被半胱胺不可逆地灭活。
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本文引用的文献
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