Mass spectrometric analysis of rat ovary and testis cytosolic glutathione S-transferases (GSTs): identification of a novel class-alpha GST, rGSTA6*, in rat testis. Export

@article{citeulike:1576940, abstract = {Cytosolic glutathione S-transferases (GSTs) from rat ovaries and testis were purified by a combination of GSH and S-hexylglutathione affinity chromatography. The isolated GSTs were subjected to reverse-phase HPLC, electrospray MS and N-terminal peptide sequencing analysis. The major GST isoenzymes expressed in ovaries are subunits A3, A4, M1, M2 and P1. Other isoenzymes detected are subunits A1, M3 and M6*. In rat testis, the major GST isoenzymes expressed are subunits A3, M1, M2, M3, M5* and M6*. Subunits A1, A4 and P1 are expressed in lesser amounts. We could not detect post-translational modifications of any GSTs with known cDNA sequence. The molecular masses of subunits M5* and M6*, two class-Mu GSTs that have not been cloned, were determined to be 25495 and 26538 Da respectively. An N-terminally modified protein from rat testis with molecular mass 25737 Da was isolated from the S-hexylglutathione column. Results from internal peptide sequencing analysis indicate that this is a novel class-Alpha GST that has not been previously reported. We designate this protein rGSTA6*.}, address = {Institute of Molecular Biology, Academia Sinica, Taipei 11529, Taiwan, Republic of China.}, author = {Hsieh, C. H. and Tsai, S. P. and Yeh, H. I. and Sheu, T. C. and Tam, M. F.}, citeulike-article-id = {1576940}, citeulike-linkout-0 = {http://view.ncbi.nlm.nih.gov/pubmed/9163345}, citeulike-linkout-1 = {http://www.hubmed.org/display.cgi?uids=9163345}, issn = {0264-6021}, journal = {Biochem J}, keywords = {cytosol, gst, gstm5, ovary, rat, rgsta6, testis}, month = {April}, pages = {503--510}, posted-at = {2007-08-20 15:12:04}, priority = {2}, title = {Mass spectrometric analysis of rat ovary and testis cytosolic glutathione S-transferases (GSTs): identification of a novel class-alpha GST, rGSTA6*, in rat testis.}, url = {http://view.ncbi.nlm.nih.gov/pubmed/9163345}, volume = {323 ( Pt 2)}, year = {1997} }

TY - JOUR ID - citeulike:1576940 L3 - citeulike-article-id:1576940 N2 - Cytosolic glutathione S-transferases (GSTs) from rat ovaries and testis were purified by a combination of GSH and S-hexylglutathione affinity chromatography. The isolated GSTs were subjected to reverse-phase HPLC, electrospray MS and N-terminal peptide sequencing analysis. The major GST isoenzymes expressed in ovaries are subunits A3, A4, M1, M2 and P1. Other isoenzymes detected are subunits A1, M3 and M6*. In rat testis, the major GST isoenzymes expressed are subunits A3, M1, M2, M3, M5* and M6*. Subunits A1, A4 and P1 are expressed in lesser amounts. We could not detect post-translational modifications of any GSTs with known cDNA sequence. The molecular masses of subunits M5* and M6*, two class-Mu GSTs that have not been cloned, were determined to be 25495 and 26538 Da respectively. An N-terminally modified protein from rat testis with molecular mass 25737 Da was isolated from the S-hexylglutathione column. Results from internal peptide sequencing analysis indicate that this is a novel class-Alpha GST that has not been previously reported. We designate this protein rGSTA6*. JF - Biochem J SN - 0264-6021 AD - Institute of Molecular Biology, Academia Sinica, Taipei 11529, Taiwan, Republic of China. EP - 510 TI - Mass spectrometric analysis of rat ovary and testis cytosolic glutathione S-transferases (GSTs): identification of a novel class-alpha GST, rGSTA6*, in rat testis. VL - 323 ( Pt 2) SP - 503 KW - cytosol KW - gst KW - gstm5 KW - ovary KW - rat KW - rgsta6 KW - testis AU - Hsieh, CH AU - Tsai, SP AU - Yeh, HI AU - Sheu, TC AU - Tam, MF PY - 1997/04/15/ UR - http://view.ncbi.nlm.nih.gov/pubmed/9163345 ER -