title: Purification and some properties of four glutathione-S-transferase isoenzymes from rat testes.
abstract: Two anionic and two cationic glutathione-S-transferase (GST) isoenzymes were found in rat testes and purified to electrophoretic homogeneity. The enzymes are heterodimers with molecular weights of about 44 000 daltons and with widely overlapping specifities for electrophilic substrates. Only one isoenzyme yielded a positive immunoprecipitation reaction with antiserum against hepatic GST-B. The reactions with antiserum against hepatic GST-A were all negative. The Michaelis and association constants for some substrates were also determined.
mesh_terms: D000818:Animals; D005982:Glutathione Transferase / Q000302:isolation & purification / Q000378:metabolism*; D007163:Immunosorbent Techniques; D007527:Isoenzymes / Q000302:isolation & purification / Q000378:metabolism*; D008099:Liver / Q000201:enzymology; D046911:Macromolecular Substances; D008297:Male; D008970:Molecular Weight; D051381:Rats; D011919:Rats, Inbred Strains; D013737:Testis / Q000201:enzymology*
chemical_list: D007527:Isoenzymes; D046911:Macromolecular Substances; D005982:Glutathione Transferase