title: 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(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).
mesh_terms: D000328:Adult; D000368:Aged; D000369:Aged, 80 and over; D003600:Cytosol / Q000201:enzymology; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D005982:Glutathione Transferase / Q000037:antagonists & inhibitors / Q000302:isolation & purification*; D006801:Humans; D005779:Immunodiffusion; D007668:Kidney / Q000201:enzymology*; D008099:Liver / Q000201:enzymology; D008297:Male; D008875:Middle Aged; D010920:Placenta / Q000201:enzymology; D011247:Pregnancy; D011506:Proteins / Q000302:isolation & purification
chemical_list: D011506:Proteins; D005982:Glutathione Transferase