Glutathione S-transferase from bovine tissues: relationship between multiple forms, distribution and catalytic activity.
Cytosolic functions obtained from various bovine tissues was individually subjected to column isoelectric focusing in order to resolve the glutathione S-transferase isoenzymes. The results showed a large variability in the isoenzyme pattern. All the tissues were found to have neutral-acidic forms of the enzyme, whilst liver, adrenal gland, testicle, lung and kidney contained a conspicuous amount of activity associated with the cationic forms of the enzyme. In spite of these differences, by comparison of the conjugating activity of transferases, we did not find essential inter-organ variations. Conversely, when the same tissue samples were tested for selenium independent glutathione peroxidase activity, using cumene hydroperoxide as second substrate, we observed a higher activity in the organs having the cationic form of glutathione S-transferase.
D000818:Animals; D001555:Benzene Derivatives / Q000378:metabolism; D002412:Cations; D002417:Cattle; D005982:Glutathione Transferase / Q000378:metabolism*; D006861:Hydrogen Peroxide / Q000378:metabolism; D007527:Isoenzymes / Q000378:metabolism*; D008297:Male; D012643:Selenium / Q000378:metabolism; D014018:Tissue Distribution
D001555:Benzene Derivatives; D002412:Cations; D007527:Isoenzymes; D006861:Hydrogen Peroxide; D005982:Glutathione Transferase; D012643:Selenium; C007164:cumene hydroperoxide