Hong Giaming, Chien Yi-Chih, Chien Cheng-I
Department of Environmental Engineering and Science, Feng Chia University, P.O. Box 25-223, Taichung 407, Taiwan.
Curr Microbiol. 2003 Oct;47(4):352-4. doi: 10.1007/s00284-002-3977-1.
Cytosolic glutathione transferases of Proteus vulgaris were purified by affinity chromatography and characterized by two-dimensional gel electrophoresis. Four different subunits were identified, and each subunit contained a different molecular mass, ranging from 26.2 kDa to 28.5 kDa; a different pI value, ranging from 8.2 to 9.4; and a different amount of protein fraction, ranging from 10% to 56%. All four subunits existed as basic proteins (pI > 7.0). From these results, we concluded that multiple forms of glutathione transferase enzymes existed in Proteus vulgaris, and four different glutathione transferase subunits were separated by 2-D gel electrophoresis.
普通变形杆菌的胞质谷胱甘肽转移酶通过亲和层析进行纯化，并通过二维凝胶电泳进行表征。鉴定出四种不同的亚基，每个亚基具有不同的分子量，范围从26.2 kDa到28.5 kDa；不同的pI值，范围从8.2到9.4；以及不同的蛋白分数，范围从10%到56%。所有四个亚基均以碱性蛋白形式存在（pI > 7.0）。从这些结果中，我们得出结论，普通变形杆菌中存在多种形式的谷胱甘肽转移酶，并且通过二维凝胶电泳分离出了四种不同的谷胱甘肽转移酶亚基。
