| Literature DB >> 9677335 |
M F Tam1, C H Hsieh, S P Tsai, T C Tam.
Abstract
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.Entities:
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Year: 1998 PMID: 9677335 PMCID: PMC1219639 DOI: 10.1042/bj3330735
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857