Abstract
The properties of horseradish peroxidase in sodium dodecyl sulfate (DDS) reversed micelles in benzene-pentanol-water solutions are studied. The potential of the analytical application of direct and reversed DDS micelles is demonstrated using newly developed methods for the determination of peroxidase substrates (hydrogen peroxide and cystein), inhibitor (sulfanylamide), and activator (imidazole) via the oxidation of o-dianisidine (o-D) with hydrogen peroxide.
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