title: The identity of the binding sites of bile salts on bovine serum albumin.
abstract: The binding of hydroxy and keto bile salts to bovine serum albumin was studied using probes for the so-called site I, II, bilirubin and fatty acids. Lithocholate, cholanate-3-one and cholanate-3,6-dione produced an interference in the energy transfer process between the albumin-tryptophan residues and the fluorescence markers of sites I and II. The results showed that site II is the binding site for the bile salts on bovine serum albumin. The binding produced a conformational change at site I, bilirubin and fatty acid binding sites, suggesting that these sites may overlap with site II.
authors.affiliation: Departamento de Ciencias Exactas, Facultad de Ciencias Bioquímicas y Farmaceuticas, Rosario, Argentina.
authors.forename: B
authors.initials: B
authors.lastname: Farruggia
authors.forename: G
authors.initials: G
authors.lastname: Picó
mesh_terms: D000818:Animals; D001647:Bile Acids and Salts / Q000378:metabolism*; D001663:Bilirubin / Q000378:metabolism; D001665:Binding Sites; D002417:Cattle; D005227:Fatty Acids / Q000378:metabolism; D005456:Fluorescent Dyes; D007700:Kinetics; D008024:Ligands; D012709:Serum Albumin / Q000378:metabolism*; D013329:Structure-Activity Relationship; D014212:Tretinoin / Q000378:metabolism
chemical_list: D001647:Bile Acids and Salts; D005227:Fatty Acids; D005456:Fluorescent Dyes; D008024:Ligands; D012709:Serum Albumin; D014212:Tretinoin; D001663:Bilirubin