Alteration of glutathione transferase isoenzyme concentrations in human renal carcinoma.
Glutathione transferase (GST) activity in the cytosolic fractions of four renal cortex tumors was found to be lower (1.85-3.4 times) than that present in the corresponding non-tumor cytosolic fractions. Glutathione transferase of both tumor and non-tumor kidney was purified by affinity chromatography and separated into five peaks at pH 4.7, 8.0, 8.4, 8.7 and 9.0 by isoelectric focusing. In the chromatogram of tumor tissues, the activity associated with the 'acidic' peak increased significantly, whereas the activities associated with 'basic' peaks all decreased in comparison with the corresponding peaks of non-tumor tissues. The acidic GST of human kidney is immunologically identical to GST pi, confirming that it is a good marker for human tumors.
D000368:Aged; D003600:Cytosol / Q000201:enzymology; D005260:Female; D005982:Glutathione Transferase / Q000302:isolation & purification / Q000378:metabolism*; D006801:Humans; D007527:Isoenzymes / Q000302:isolation & purification / Q000378:metabolism*; D007672:Kidney Cortex / Q000201:enzymology; D007680:Kidney Neoplasms / Q000473:pathology*; D007700:Kinetics; D008297:Male; D008875:Middle Aged
D007527:Isoenzymes; D005982:Glutathione Transferase