硫代磷酸三烷基酯与谷胱甘肽S-转移酶

Trialkyl phosphorothioates and glutathione S-transferases.

作者信息

Aldridge W N, Grasdalen H, Aarstad K, Street B W, Norkov T

出版信息

Chem Biol Interact. 1985 Jul;54(2):243-56. doi: 10.1016/s0009-2797(85)80166-6.

Abstract

Using a rat liver cytosol source of enzyme trialkyl phosphorothioates have been shown to be substrates of glutathione S-transferases. Using OSS-trimethyl phosphorodithioate (OSS-Me(O] and OOS-trimethyl phosphorothioate (OOS-Me(O] the methyl transferred to the sulphydryl of glutathione is that attached to phosphorus via an oxygen atom. Fractionation of liver cytosol has shown that although the bulk activity is due to the three isozymes (1-1; 3-4; 1.2), OSS-Me(O) is a general substrate for glutathione S-transferases. The specific activity is low compared with the substrates 1-chloro-2,4-dinitrobenzene and 1,2-dichloro-4-nitrobenzene.

摘要

使用大鼠肝脏胞质溶胶来源的酶，已证明三硫代磷酸酯是谷胱甘肽S-转移酶的底物。使用双硫代磷酸三甲酯（OSS-Me(O]）和硫代磷酸三甲酯（OOS-Me(O]）时，转移到谷胱甘肽巯基上的甲基是通过氧原子与磷相连的那个甲基。肝脏胞质溶胶的分级分离表明，尽管大部分活性归因于三种同工酶（1-1；3-4；1.2），但OSS-Me(O]是谷胱甘肽S-转移酶的通用底物。与底物1-氯-2,4-二硝基苯和1,2-二氯-4-硝基苯相比，其比活性较低。