Ordinary tight-binding inhibition in steady-state enzyme systems is conveniently evaluated by means of the Henderson plot. This is a linear plotting form that has an ordinate intercept equal to the total enzyme concentration. However, there are two experimental situations that yield deviations from
The sulfur-cyanolysis sites of serum albumin: Metabolite competition studies
โ Scribed by Jarabak, Rebecca ;Westley, John
- Book ID
- 102875586
- Publisher
- John Wiley and Sons
- Year
- 1989
- Tongue
- English
- Weight
- 699 KB
- Volume
- 4
- Category
- Article
- ISSN
- 0887-2082
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โฆ Synopsis
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 multipIe 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.
๐ SIMILAR VOLUMES
Efforts to locate the active site for sulfur cyanolysis catalyzed by bovine serum albumin have led to systematic tests of several compounds that inhibit the catalyzed reaction. Hexanoate and 5- dimethylaminonaphthalene-1-sulfonate bind at the same site and are partial inhibitors competitive with cya
The results of kinetic experiments measuring the effects of a variety of ligands on the sulfur-cyanolysis reaction catalyzed by serum albumin point to the conclusion that the active site for cyanolysis is on subdomain 3-AB. Relationships among the inhibition by short-chain fatty acids, the activatio