Abstract
By sequential use of GSH-affinity chromatography and chromatofocusing, the isoenzymes of glutathione transferase from tumor and non-tumor kidney tissues have been purified and their properties compared. On the basis of electrophoretic mobilities on SDS/polyacrylamide gel, substrate specificities toward the diagnostic substrates cumene hydroperoxide and ethacrynic acid and immunoreactivity with antisera raised against alpha, mu and pi class glutathione transferases, it was found that most of the isoenzymes purified from both tumor and non-tumor kidney can be identified as members of either alpha or pi classes. All the samples investigated lacked mu class glutathione transferase. In addition, we could identify in tumor samples two transferases GST-7.6 and GST-5.8/5.9 which on the basis of immunological properties cannot be related to any of the members of the three major classes of glutathione transferases. The latter do not appear to have corresponding forms in non-tumor tissues. It was suggested that specific transferases can be selectively expressed by tumor kidney carcinoma.
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