AMINO-ACID-SEQUENCE OF GLUTATHIONE-S-TRANSFERASE RGSTM5-ASTERISK FROMRAT TESTIS

Glutathione S-transferase rGSTM5 was isolated from rat testis with a combination of glutathione affinity column and reverse-phase column ch romatography. The protein was digested with Achromobacter protease I o r endoproteinase Arg-C. The peptide fragments were isolated for electr ospray MS and N-terminal peptide sequencing analyses. The primary amin o 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-translationa lly modified.