PURIFICATION AND CHARACTERIZATION OF 2 GLUTATHIONE S-ARYLTRANSFERASE ACTIVITIES FROM RAT-LIVER
PURIFICATION AND CHARACTERIZATION OF 2 GLUTATHIONE S-ARYLTRANSFERASE ACTIVITIES FROM RAT-LIVER
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DOI：
10.1042/bj1470513
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发表时间：
1975-01-01
影响因子：
4.1
通讯作者：
MANNERVIK, B
中科院分区：
文献类型：
--
作者：
ASKELOF, P;GUTHENBERG, C;MANNERVIK, B
从大鼠肝脏中纯化出两种形式的谷胱甘肽s -芳基转移酶。两种形式之间唯一的区别是在色谱和电泳性质，这允许两个物种的分离。酶及其亚基的分子量估计分别为50000和23000左右。当一种底物浓度不变而另一种底物浓度变化时，稳态动力学不遵循Michaelis-Menten动力学。几种s取代的谷胱甘肽衍生物被测试为酶反应的抑制剂。巯基试剂使酶失活。
Two forms of glutathione S-aryltransferase were purified from rat liver. The only differences noted between the two forms were in the chromatographic and electrophoretic properties, which permitted the separation of the two species. The molecular weights of the enzyme and its subunits were estimated as about 50000 and 23000 respectively. The steady-state kinetics did no follow Michaelis-Menten kinetics when one substrate concentration was kept constant while the second substrate concentration was varied. Several S-substituted GSH derivatives were tested as inhibitors of the enzymic reaction. The enzyme was inactivated by thiol-group reagents.