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Competitive partial inhibitors of serum albumin-catalyzed sulfur cyanolysis

✍ Scribed by Jarabak, Rebecca ;Westley, John

Book ID: 102875587
Publisher: John Wiley and Sons
Year: 1990
Tongue: English
Weight: 702 KB
Volume: 5
Category: Article
ISSN: 0887-2082
DOI: 10.1002/jbt.2570050102

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✦ Synopsis

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 cyanide, uncompetitive with respect to sulfur. Various dansyl amino acids and 1-anilino-&naphthalene sulfonate display the same inhibitory behavior but bis (1-anilino-&naphthalene sulfonate) is a total inhibitor competitive with cyanide. These findings are interpreted to indicate that the cyanolysis active site is near, but not at, one of the short-chain fatty acid binding sites on albumin subdomain 2-AB or 3-AB. Both ionic repulsion and steric considerations are implicated in the mechanisms of inhibition.

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