Tam M F, Hsieh C H, Tsai S P, Tam T C
Institute of Molecular Biology, Academia Sinica, Taipei 11529, Republic of China.
Biochem J. 1998 Aug 1;333 ( Pt 3)(Pt 3):735-9. doi: 10.1042/bj3330735.
Glutathione S-transferase rGSTM5* was isolated from rat testis with a combination of glutathione affinity column and reverse-phase column chromatography. The protein was digested with Achromobacter protease I or endoproteinase Arg-C. The peptide fragments were isolated for electrospray MS and N-terminal peptide sequencing analyses. The primary amino acid sequence of rGSTM5* comprises 217 residues and has a calculated average molecular mass of 25495.3 Da. The result is identical to that obtained for rGSTM5* with liquid chromatography-MS from a mixture of rat testicular GSTs. Therefore, rGSTM5* has not been post-translationally modified.
谷胱甘肽S-转移酶rGSTM5是通过谷胱甘肽亲和柱和反相柱色谱相结合的方法从大鼠睾丸中分离出来的。该蛋白质用无色杆菌蛋白酶I或内肽酶Arg-C进行消化。分离肽片段用于电喷雾质谱和N端肽测序分析。rGSTM5的一级氨基酸序列由217个残基组成,计算得出的平均分子量为25495.3道尔顿。该结果与从大鼠睾丸谷胱甘肽S-转移酶混合物中通过液相色谱-质谱法获得的rGSTM5结果一致。因此,rGSTM5未发生翻译后修饰。