A comparison of the subcellular distribution, subunit composition and bile acid-binding activity of glutathione S-transferases from trout and rat liver

Abstract

1. 1. More than 90% of the glutathione S-transferase activity in both trout and rat liver is in cytosol. The activity in the microsomal fraction of rat but not trout liver is stimulated by iodoacetamide. 2. 2. The trout liver enzymes are dimers. The molecular weights of their monomers are similar to those of the Ya (22,000) and Yb (23,500) monomers of the rat liver enzymes. 3. 3. Unlike the enzymes from rat liver, those from trout liver do not bind glycocholate. 4. 4. Trout liver contains a species (15,000) that does bind glycocholate.