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pubmed-article:1805098pubmed:abstractTextCetyltrimethylammonium and n-octadecyldimethylsulfonium bromides inhibit the Clostridium perfringens phospholipase C-catalyzed hydrolysis of 1-S-phosphocholine-2-O-hexadecanoyl-1-mercapto-2-ethanol (1) at pH 7.5, 37 degrees C, mu = 0.15 with KCl. Mixed micelles containing 1 and either inhibitor are substrates for the enzyme and the fraction of activity remaining is a monotonic, but non-linear function of the mole fraction of inhibitor. Simple saturation kinetics are observed as the concentration of 1 is increased in mixed micelles containing a constant mole fraction of inhibitor. Inhibition constants for cetyltrimethylammonium and n-octadecyldimethylsulfonium bromides are 0.66 +/- 0.04 and 0.25 +/- 0.02 mM, respectively. The data suggest that the significant inhibition previously observed for soluble alkyldisulfonium salts (K50 for dodecamethylene-bis(dimethylsulfonium) bromide, 27 microM) is dependent upon bifunctional cationic interactions rather than hydrophobic binding.lld:pubmed
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pubmed-article:1805098pubmed:authorpubmed-author:McMahonR FRFlld:pubmed
pubmed-article:1805098pubmed:authorpubmed-author:SnyderW RWRlld:pubmed
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pubmed-article:1805098pubmed:pagination957-9lld:pubmed
pubmed-article:1805098pubmed:dateRevised2007-11-15lld:pubmed
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pubmed-article:1805098pubmed:articleTitleInhibition of the Clostridium perfringens phospholipase C hydrolysis of a thiophosphate analog of lysophosphatidylcholine by micelle-bound ammonium and sulfonium cations.lld:pubmed
pubmed-article:1805098pubmed:affiliationDepartment of Chemistry, University of Illinois, Chicago 60680.lld:pubmed
pubmed-article:1805098pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:1805098pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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