The sulfur-cyanolysis sites of serum albumin: metabolite competition studies.
In the presence of a source of sulfane sulfur, a cyanolysis reaction catalyzed by serum albumin may contribute to cyanide detoxication. The active site for this catalysis by serum albumin has been investigated in competition studies with ligands that have known albumin binding sites. Despite complications caused by the occurrence of multiple primary and secondary sites for many ligands, the results show that the primary sites for bilirubin, steroids, indoles, aspirin, and palmitate are distinct from that for sulfur. Laurate is a tight-binding partial inhibitor of the cyanolysis reaction, competitive with cyanide rather than with sulfur. In view of the formal mechanism previously established for the catalyzed reaction, this result indicates that the sulfur-cyanolysis site is probably near the site occupied by laurate.
Jarabak
R
R
Department of Biochemistry and Molecular Biology, University of Chicago, Illinois 60637.
Westley
J
J
D001241:Aspirin / Q000097:blood; D001663:Bilirubin / Q000097:blood; D001667:Binding, Competitive / Q000502:physiology; D002384:Catalysis; D003486:Cyanides / Q000097:blood*; D004958:Estradiol / Q000097:blood; D007700:Kinetics; D007848:Laurates / Q000097:blood; D010168:Palmitates / Q000097:blood; D011485:Protein Binding; D012710:Serum Albumin, Bovine / Q000378:metabolism*; D013455:Sulfur / Q000097:blood*; D014364:Tryptophan / Q000097:blood
D003486:Cyanides; D007848:Laurates; D010168:Palmitates; D012710:Serum Albumin, Bovine; D004958:Estradiol; D013455:Sulfur; D014364:Tryptophan; D001241:Aspirin; D001663:Bilirubin