CLEAVAGE OF HEME FROM HORSERADISH PEROXIDASE BY METHANOL WITH INHIBITION OF ENZYMIC ACTIVITY
نویسندگان
چکیده
منابع مشابه
Mechanism of inhibition of horseradish peroxidase by cyclopropanone hydrate.
Cyclopropanone hydrate irreversibly inactivates horseradish peroxidase in a time-dependent manner in the presence of oxidizing agent, hydrogen peroxide. The inhibition reaction is a second order reaction of cyclopropanone hydrate with compound I, the 2 electron-oxidized form of peroxidase, and results in covalent modification of the heme cofactor. A new propionic acid side chain is substituted ...
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Incubation of horseradish peroxidase with phenylhydrazine and H2O2 markedly depresses the catalytic activity and the intensity, but not position, of the Soret band. Approximately 11-13 mol of phenylhydrazine and 25 mol of H2O2 are required per mol of enzyme to minimize the chromophore intensity. The enzyme retains some activity after such treatment, but this activity is eliminated if the enzyme...
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Horseradish peroxidase (HRP) mediates efficient conversion of many phenolic contaminants and thus has potential applications for pollution control. Such potentially important applications suffer however from the fact that the enzyme becomes quickly inactivated during phenol oxidation and polymerization. The work here provides the first experimental data of heme consumption and iron releases to ...
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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...
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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 ...
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ژورنال
عنوان ژورنال: Journal of Histochemistry & Cytochemistry
سال: 1974
ISSN: 0022-1554,1551-5044
DOI: 10.1177/22.9.908