The identity of the binding sites of bile salts on bovine serum albumin

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 a...

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Bibliographic Details
Published in:	Research communications in chemical pathology and pharmacology Vol. 80; no. 2; p. 234
Main Authors:	Farruggia, B, Picó, G
Format:	Journal Article
Language:	English
Published:	United States 01-05-1993
Subjects:	Animals Bile Acids and Salts - metabolism Bilirubin - metabolism Binding Sites Cattle Fatty Acids - metabolism Fluorescent Dyes Kinetics Ligands Serum Albumin - metabolism Structure-Activity Relationship Tretinoin - metabolism
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Summary:	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.
ISSN:	0034-5164