兔红细胞谷胱甘肽还原酶的分离及某些特性（38548）

Isolation and some characteristics of glutathione reductase from rabbit erythrocytes (38548).

作者信息

Ray L E, Prescott J M

出版信息

Proc Soc Exp Biol Med. 1975 Feb;148(2):402-9. doi: 10.3181/00379727-148-38548.

Abstract

Glutathione reductase from rabbit erythrocytes was pruified to homogeneity and found to be a monomer with a mol wt of 60,000. Both NADPH and HADH were capable of acting as cofactors for the reduction of GSSG and the following kinetic values were obtained: Km, GSSG = 120 muM; Km, NADPH = 37 muM; Vmax = 23 mumoles NADPH/min/mg protein, Km, NADH = 420 muM; Vmax = 3 mumoles NADH/min/mg protein. Rabbit erythrocyte GR exhibited substrate inhibition, and was susceptible to inhibition by p-hydroxymercuribenzoate under certain conditions.

摘要

兔红细胞谷胱甘肽还原酶被纯化至同质，发现它是一种分子量为60,000的单体。NADPH和HADH都能够作为还原GSSG的辅因子，并获得了以下动力学值：Km，GSSG = 120 μM；Km，NADPH = 37 μM；Vmax = 23微摩尔NADPH/分钟/毫克蛋白质，Km，NADH = 420 μM；Vmax = 3微摩尔NADH/分钟/毫克蛋白质。兔红细胞谷胱甘肽还原酶表现出底物抑制作用，并且在某些条件下易受对羟基汞苯甲酸的抑制。