Iizuka M, Inoue Y, Murata K, Kimura A
Research Institute for Food Science, Kyoto University, Japan.
J Bacteriol. 1989 Nov;171(11):6039-42. doi: 10.1128/jb.171.11.6039-6042.1989.
Glutathione S-transferase was purified approximately 2,300-fold from cell extracts of Escherichia coli B with a 7.5% activity yield. The molecular weight of the enzyme was 45,000, and the enzyme appeared to consist of two homogeneous subunits. The enzyme was almost specific to 1-chloro-2,4-dinitrobenzene (Km, 1.43 mM) and glutathione (Km, 0.33 mM). The optimal pH and optimal temperature for activity were 7.0 and 50 degrees C, respectively, and the enzyme was stable from pH 5 to 11. The activity of the enzyme for 1-chloro-2,4-dinitrobenzene (3,2 mumol/min per mg of protein) was significantly lower than those of the enzymes from mammals, plants, and fungi.
谷胱甘肽S-转移酶从大肠杆菌B的细胞提取物中纯化了约2300倍，活性产率为7.5%。该酶的分子量为45000，似乎由两个同质亚基组成。该酶对1-氯-2,4-二硝基苯（Km，1.43 mM）和谷胱甘肽（Km，0.33 mM）几乎具有特异性。活性的最佳pH和最佳温度分别为7.0和50℃，该酶在pH 5至11范围内稳定。该酶对1-氯-2,4-二硝基苯的活性（每毫克蛋白质3.2 μmol/min）明显低于哺乳动物、植物和真菌来源的酶。
