Add time:07/13/2019 Source:sciencedirect.com
1.1. The effect of a cation active quaternary ammonium salt, domiphen bromide (dodecyldimethyl(2-phenoxyethyl)ammonium bromide), on the enzymic hydrolysis of certain N-l-aminoacyl-2-naphthylamines and p-nitrophenyl phosphate was investigated. The enzymes studied included commercial trypsin, chymotrypsin, subtilisin, papain, leucine aminopeptidase and Escherichia coli alkaline phosphatase, and purified rat-liver aminopeptidase B, and other enzyme preparations derived from various mammalian and bacterial sources.2.2. Domiphen bromide strongly inhibited the aminopeptidase-like enzymes, though less so the E. coli alkaline phosphatase. The several plots constructed revealed that the inhibition probably has a basically noncompetitive nature.3.3. Domiphen bromide had no effect on the trypsin- and subtilisin-catalyzed reactions, but the activity of α-chymotrypsin was strongly increased at approx. 0.5 mM affector concentrations, while higher and lower concentration caused inhibition.4.4. The results showed that domiphen bromide can be used as a selective affector in enzyme studies. An explanation of its mode of action was attempted in terms of the known reactions of surfaceactive agents to proteins in general, rather than a reaction to a specific amino acid residue at or close to the active site. The suggestion is supported by the observed correlation between the inhibitory effect and the isoelectric point of the enzymes investigated.
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