Partial purification of two lithocholic acid-binding proteins from rat liver 100000g supernatants

Abstract
The partial purification of 2 lithocholic acid-binding proteins from liver 100,000 g supernatants is described. Gel-filtration, (NH4)2SO4 fractionation. Ca3(PO4)2 fractionation and ion-exchange chromatography were used. Both proteins exhibited glutathione S-transferase activity; one may be the non-specific anion-binding protein ligandin. Glutathione S-transferase activity of one of the binding proteins was inhibited by lithocholic acid.