Purification and characterization of glutathione S-transferases in human kidney

Abstract 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(π) in human liver previously characterized by us [1], by SDS-polyacrylamide slab gel electrophoresis, two-dimensional gel electrophoresis and double immunodiffusion. GST III (μ) was not detected in any of 5 specimens examined. GST-π 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 μg/g of tissue; 0.27% of the total cytosol protein amount. In many organs including the placenta, GST-π is present at levels similar to that in the kidney but low in the liver (34 μg/g).