Glutathione S-transferase activity from guinea-pig brain: a comparison with hepatic multiple forms.
1. Specific activities of glutathione S-transferase towards four model substrates were determined in guinea-pig brain 50,000 g supernatant and compared with those obtained for liver and kidney extract. 2. By using 1-chloro-2,4-dinitrobenzene as substrate, glutathione S-transferase activity was measured in different anatomical regions of brain; cerebellum expressed the highest conjugating capacity. 3. Brain glutathione S-transferase was resolved into four major peaks (PI 6.10, 6.60, 7.15, 7.65) each having similar kinetic constants for both substrates GSH and 1-chloro-2,4-dinitrobenzene. 4. Likewise, four forms, focused at pH 6.45, 7.14, 7.50 and 8.88, were obtained from liver. 5. Unlike hepatic tissue, brain does not possess the highly alkaline form which displays Se-independent GSH peroxidase activity. 6. Several psychotropic agents, including chlorpromazine and chlorazepate, produced a considerable in vitro inhibition on brain transferase activity.
D000818:Animals; D001921:Brain / Q000201:enzymology*; D002850:Chromatography, Gel; D003600:Cytosol / Q000201:enzymology; D005260:Female; D005982:Glutathione Transferase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D006168:Guinea Pigs; D005779:Immunodiffusion; D066298:In Vitro Techniques; D007525:Isoelectric Focusing; D007527:Isoenzymes / Q000378:metabolism; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D011619:Psychotropic Drugs / Q000494:pharmacology
D007527:Isoenzymes; D011619:Psychotropic Drugs; D005982:Glutathione Transferase