Soluble glutathione S-transferases from rat testes: isoenzyme pattern and lack of inducibility by drug metabolizing enzyme inducers.
The soluble glutathione S-transferase (GST) isoenzymes from rat testicular tissue were separated in one chromatographic run on carboxymethyl cellulose. GST was measured with 1-chloro-2,4-dinitrobenzene as the second substrate. The following percentages for the different isoenzymes were found: GST AA: 12.6%, GST A:8.1%, GST B:4.2%, GST C:18.1%, GST D and E: not detected, GST x:7.4%, and anionic GST:49.6%. These values were quite different from those found in liver tissue. Testicular GST could not be induced by the drug metabolizing enzyme inducers trans-stilbene oxide, DDT, and phenobarbital. The high GST content in rat testes may suggest that these enzymes function also in this tissue in the metabolism and detoxification of electrophilic xenobiotics.
D000818:Animals; D004790:Enzyme Induction / Q000187:drug effects*; D005982:Glutathione Transferase / Q000032:analysis* / Q000096:biosynthesis; D007527:Isoenzymes / Q000032:analysis / Q000096:biosynthesis; D008099:Liver / Q000201:enzymology; D008297:Male; D051381:Rats; D011919:Rats, Inbred Strains; D013737:Testis / Q000201:enzymology*
D007527:Isoenzymes; D005982:Glutathione Transferase