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
Localization of the sulfur-cyanolysis site of serum albumin to subdomain 3-ab
β Scribed by Jarabak, Rebecca ;Westley, John
- Publisher
- John Wiley and Sons
- Year
- 1991
- Tongue
- English
- Weight
- 469 KB
- Volume
- 6
- Category
- Article
- ISSN
- 0887-2082
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β¦ Synopsis
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 activation by p-nitrophenyl acetate, and the influence of bilirubin and L-tryptophan on these effects indicate that the cyanolysis active site and the known primary binding site for indoles are both near, but on opposite sides of, tyrosine-409 of bovine albumin (tyrosine-411 of human albumin).
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