The Reaction of Coumarins with Horseradish Peroxidase
نویسندگان
چکیده
منابع مشابه
The reaction of ferrous horseradish peroxidase with hydrogen peroxide.
Hydrogen peroxide reacts with ferrous horseradish peroxidase and converts it to oxyperoxidase in a sequence of two reactions. The first is the reaction of ferrous peroxidase with HzOz to form Compound II; the second is the reaction of Compound II with HzOz to form oxyperoxidase. Both reactions follow second order kinetics, being first order with respect to each of the reactants. They proceed wi...
متن کاملStoichiometry of the reaction between horseradish peroxidase and p-cresol.
Over a wide range of pH horseradish peroxidase compound I can be reduced quantitatively via compound II to the native enzyme by only 1 molar equivalent of p-cresol. Since 2 molar equivalents of electrons are required for the single turnover of the enzymatic cycle, p-cresol behaves as a 2-electron reductant. With p-cresol and compound I in a 1:1 ratio compound II and p-methylphenoxy radicals are...
متن کاملIn Vitro Study of Acriflavine Interaction with Horseradish Peroxidase C
Acriflavine (3,6-diaminoacridine) is an anticeptic drug developed in 1912. Previous research has focused on investigation of the intercalating features of acriflavine, but little is known about its interaction with proteins. Drug-receptor interaction is of major interest in clinical science. The aim of the present study was to evaluate the ability of acriflavine to induce alterations in conform...
متن کاملRemoval of Phenols with Encapsulated Horseradish Peroxidase in Calcium Alginate
Horseradish peroxidase was encapsulated in calcium alginate for the purpose of phenol removal. Considering enzyme encapsulation efficiency, retention activity and enzyme leakage of the capsules, the best gelation condition was found to be 1 % w/v of sodium alginate solution and 5.5 % w/v of calcium chloride hexahydrate. Upon immobilization, pH profile of enzyme activity changes as it shows ...
متن کاملStabilization of the substrate reaction of horseradish peroxidase with o-phenylenediamine in the enzyme immunoassay.
When the horseradish peroxidase reaction is stopped with acid, the decay of unconverted hydrogen peroxide is responsible for the further oxidation of o-phenylenediamine. This leads to a time-dependent flattening of the standard curve in the enzyme immunoassay, after the reaction has been stopped. Addition of reducing agents, such as sulphite ions, to the stopping solution, prevents the further ...
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ژورنال
عنوان ژورنال: Plant Physiology
سال: 1975
ISSN: 0032-0889,1532-2548
DOI: 10.1104/pp.55.1.35