Madelian V, Warren W A
Res Commun Chem Pathol Pharmacol. 1977 Feb;16(2):385-8.
Partial purification from rat liver of an enzyme which catalyzes defluorination of methoxyflurane is described. Fractionation of liver homogenates by protamine sulfate and ammonium sulfate precipitation and by Sephadex G-100 chromatography results in a 10-fold purification with 53% recovery. The enzyme requires glutathione for activity, and other sulfhydrhyl compounds cannot be substituted. The enzyme appears to be a glutathione S-transferase, possibly one of several which have recently been characterized.
本文描述了从大鼠肝脏中对一种催化甲氧氟烷脱氟的酶进行部分纯化的过程。通过硫酸鱼精蛋白和硫酸铵沉淀以及葡聚糖凝胶G - 100柱色谱对肝脏匀浆进行分级分离，得到了10倍的纯化倍数，回收率为53%。该酶的活性需要谷胱甘肽，其他巯基化合物不能替代。该酶似乎是一种谷胱甘肽S - 转移酶，可能是最近已被鉴定的几种酶之一。
