Identification of a new glutathione S-transferase from rat liver cytosol.
A new glutathione S-transferase has been purified to homogeneity from 105,000 X g supernatant of Sprague-Dawley rat liver homogenates. The purified enzyme exhibited specific activities of approximately 1.8, and 0.12 mumoles X min-1 X mg-1 toward 1-chloro 2,4-dinitrobenzene and cumene hydroperoxide respectively. The SDS gel electrophoresis data on subunit composition revealed that the new transferase is composed of two subunits with an identical Mr of 24,400 (Y alpha Family). Our in vitro translation experiments with rat liver poly(A) RNAs and substrate specificity data suggest that this subunit is different from the previously reported Ya , Yb and Yc subunits of rat liver glutathione S-transferases. Comparatively, the new isozyme showed significant activity toward 1,2 epoxy-3-(P-nitrophenoxy)-propane, ethacrynic acid and P-nitrophenyl acetate, 0.4, 0.34 and 0.18 mumoles. min-1 X mg-1 respectively.
D000818:Animals; D011232:Chemical Precipitation; D003600:Cytosol / Q000201:enzymology*; D005982:Glutathione Transferase / Q000302:isolation & purification*; D007120:Immunochemistry; D007527:Isoenzymes / Q000302:isolation & purification; D008099:Liver / Q000201:enzymology*; D008297:Male; D010779:Photofluorography; D014176:Protein Biosynthesis; D051381:Rats; D011919:Rats, Inbred Strains; D013379:Substrate Specificity
D007527:Isoenzymes; D005982:Glutathione Transferase