Purification and characterization of glutathione S-transferases in human kidney.

Four glutathione S-transferase (GST, EC 2.5.1.18) forms were purified from human kidney by S-hexylglutathione affinity chromatography followed by chromatofocusing using a fast protein liquid chromatography system. These forms were demonstrated to be identical with GSTs I, II, IV, V(pi) in human liver previously characterized by us, by SDS-polyacrylamide slab gel electrophoresis, two-dimensional gel electrophoresis and double immunodiffusion. GST III (mu) was not detected in any of 5 specimens examined. GST-pi was a major form in the kidney. The activity was 30-40% of the total activity in kidney cytosol and the protein amount was approximately 140 micrograms/g of tissue; 0.27% of the total cytosol protein amount. In many organs including the placenta, GST-pi is present at levels similar to that in the kidney but low in the liver (34 micrograms/g).