Comparison of the affinities of newly identified human bile acid binder and cationic glutathione S-transferase for bile acids.
The bile acid binding properties of the newly identified bile acid binder (Mr = 36,000) (FEBS Lett. 1984. 177: 31-35) and the major cationic glutathione (GSH) S-transferase (Mr = 50,000) in human liver cytosol were compared. Binding affinities were measured by the competitive displacement by bile acids of 1-anilino-8-naphthalene sulfonate (ANS) bound to the proteins and, in some cases, by direct methods of flow dialysis and equilibrium dialysis. The binding affinities for various bile acids by the human bile acid binder were 2-5 orders of magnitude greater than those by human cationic GSH S-transferase. This suggests an important physiologic role for the former protein in intracellular transfer of bile acids in human liver.
D000817:Anilino Naphthalenesulfonates / Q000378:metabolism; D001647:Bile Acids and Salts / Q000378:metabolism*; D001667:Binding, Competitive; D003600:Cytosol / Q000378:metabolism; D005982:Glutathione Transferase / Q000378:metabolism*; D006801:Humans; D066298:In Vitro Techniques; D007700:Kinetics; D008099:Liver / Q000378:metabolism*
D000817:Anilino Naphthalenesulfonates; D001647:Bile Acids and Salts; C027132:1-anilino-8-naphthalenesulfonate; D005982:Glutathione Transferase