Separation and characterization of glutathione s-transferases from rat liver, 1986

Analysis of the glutathione S-transferase activity from the hepatic cytosol of untreated, 3-me thylcholanth rene (MC), butylated hydroxy anisole (BHA), and BHA + MC-treated female Sprague-Dawley rats revealed that the inducers differentially stimulated this activity (when the substrates CDNB and DCNB were used), and the kinetics of the conjugation reaction were also affected. Partial purification of the cytosolic glutathione S-transferase was achieved primarily by DEAE and CM-cellulose chromatography using a step gradient of 0, 50, 100, 150mM KC1. The results showed similar chromatrographic profiles that contained one protein peak at 50mM KC1 that exhibited glutathione S-transferase activity using CDNB as the substrate. Further analysis of the protein peaks of each group revealed that the BHA and BHA + MC treatment group causes substantial increases in the protein that migrated at the reputed molecular weight of the transferase. The results suggest that BHA induces a different form of the transferase than the one induced by MC and also that BHA induces more transferase than the MC or untreated groups