Gawai K R, Pawar S S
Xenobiotica. 1984 Jul;14(7):605-7. doi: 10.3109/00498258409151456.
Glutathione-S-transferase (GST) from the liver cytosol of phenobarbital (PB)-treated rabbits was purified by DEAE-cellulose, CM-cellulose and hydroxylapatite column chromatography. Four species of GST were obtained by eluting the CM-cellulose column with a linear KCl gradient, and the major protein investigated. The purified enzyme from PB-treated and untreated rabbit had specific activities of 125.16 units/mg and 72.8 units/mg of protein, respectively, and the apparent Km was 0.6 X 10(-3) M for GSH and 1.6 X 10(-3) M for 1-chloro-2,4-dinitrobenzene. The optimum pH value was 8.7 and the enzyme was able to conjugate with 1-chloro-2,4-dinitrobenzene, 1,2-dichloro-4-nitrobenzene, 1,2-epoxy-3-(p-nitrophenoxy)propane and p-nitrobenzyl chloride.
通过DEAE - 纤维素、CM - 纤维素和羟基磷灰石柱色谱法，从苯巴比妥（PB）处理过的兔子肝脏细胞溶质中纯化谷胱甘肽 - S - 转移酶（GST）。用线性KCl梯度洗脱CM - 纤维素柱，得到四种GST，并对主要蛋白质进行了研究。来自PB处理过和未处理过的兔子的纯化酶的比活性分别为125.16单位/毫克和72.8单位/毫克蛋白质，对谷胱甘肽（GSH）的表观Km为0.6×10⁻³ M，对1 - 氯 - 2,4 - 二硝基苯的表观Km为1.6×10⁻³ M。最适pH值为8.7，该酶能够与1 - 氯 - 2,4 - 二硝基苯、1,2 - 二氯 - 4 - 硝基苯、1,2 - 环氧 - 3 -（对硝基苯氧基）丙烷和对硝基苄基氯结合。
