AN INTRACELLULAR GSH-PEROXIDASE WITH A LIPID PEROXIDE SUBSTRATE
AN INTRACELLULAR GSH-PEROXIDASE WITH A LIPID PEROXIDE SUBSTRATE
复制标题
DOI：
10.1016/0006-291x(68)90721-3
复制
发表时间：
1968-01-01
影响因子：
3.1
通讯作者：
OBRIEN, PJ
中科院分区：
文献类型：
--
作者：
LITTLE, C;OBRIEN, PJ
研究了肝脏上清液催化过氧化亚油酸氧化谷胱甘肽的动力学、产物和性质。研究发现，这主要是一种酶过氧化物酶的作用，而不是先前认为的血红蛋白（Little & O'Grien, 1967a）。过氧化物酶对硫醇类，尤其是谷胱甘肽，作为h给体具有特异性，但可能接受任何过氧化氢作为底物。与血红蛋白过氧化物酶不同，该酶不受CN−、N3−、F−或过氧化物的抑制。此外，尽管谷胱甘肽过氧化物酶对热和酸不稳定，但其活性并没有被FMN或FAD恢复，也没有被falvin类似物quinacrine抑制，因此不太可能是一种黄蛋白。n -乙基亚胺和对氯脲苯甲酸酯（pCMB）对该酶有不可逆的抑制作用，而其他硫醇类试剂对该酶无抑制作用。对酶进行了有限的纯化。
Studies have been made on the kinetics, products and properties of liver supernatant-catalyzed GSH oxidation by linoleic acid hydroperoxide (LAHPO). It was found that an enzymic peroxidase was principally involved and not the hemoprotins previously suggested (Little & O'Grien, 1967a). The peroxidase was specific for thiols, especially GSH, as H-donors, but probably accepted any hydroperoxide as substrate. Unlike hemoprotein peroxidases, the enzyme was not inhibited inhibited by CN−, N3−, F−or peroxide. Furthermore, it is unlikely that the enzyme was a flavoprotein since although GSH-peroxidase was heat and acid labile the activity was not restored by FMN or FAD, and also not inhibited by the falvin analog quinacrine. The enzyme was readily and irreversibly inhibited by N-ethylaleimide and p-chloromecuribenzoate (pCMB), but not by other thiol reagents. A limited purification of the enzyme was carried out.