Favaloro B, Melino S, Petruzzelli R, Di Ilio C, Rotilio D
Istituto di Ricerche Farmacologiche Mario Negri, Consorzio Mario Negri Sud, Gennaro Paone Environmental Health Center, Santa Maria Imbaro, Italy.
FEMS Microbiol Lett. 1998 Mar 1;160(1):81-6. doi: 10.1111/j.1574-6968.1998.tb12894.x.
Glutathione transferase was purified from Ochrobactrum anthropi and its N-terminal sequence was determined to be MKLYYKVGACSLAPHIILSEAGLPY. The apparent molecular mass of the protein (24 kDa) was determined by SDS-polyacrylamide gel electrophoresis analysis. The amino acid sequence obtained showed similarities with known bacterial glutathione transferases in the range of 72-64%. Immunoblotting experiments performed with antisera raised against glutathione transferase from O. anthropi did not show cross-reactivity with two bacterial glutathione transferases belonging to Serratia marcescens and Proteus mirabilis.
谷胱甘肽转移酶从嗜人苍白杆菌中纯化得到，其N端序列测定为MKLYYKVGACSLAPHIILSEAGLPY。通过SDS-聚丙烯酰胺凝胶电泳分析确定该蛋白质的表观分子量为24 kDa。所得氨基酸序列与已知细菌谷胱甘肽转移酶的相似性在72%-64%之间。用针对嗜人苍白杆菌谷胱甘肽转移酶产生的抗血清进行的免疫印迹实验表明，该抗血清与粘质沙雷氏菌和奇异变形杆菌的两种细菌谷胱甘肽转移酶没有交叉反应。
