Jackson R C
Biochem J. 1969 Feb;111(3):309-15. doi: 10.1042/bj1110309.
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.
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。