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Rogozhina T.V.,Yakutsk State Agricultural Academy | Rogozhin V.V.,Yakutsk State Agricultural Academy
Biomeditsinskaya Khimiya | Year: 2011

Reactions of peroxidase oxidation of triftazine and thioproperazine have been investigated in the presence of horseradish peroxidase using steady state kinetic methods. It has been shown that phenothiazines are slowly oxidizable substrates for horseradish peroxidase. kcat and Km values have been determined in the range of pH from 4.5 to 7.5. The study of co-oxidation of phenothiazines and o-dianisidinc (ODN) revealed that in the presence of aminazine and ODN in the reaction medium both substances follow sequential oxidation. ODN oxidation was not observed until full conversion of aminazine. At pH 4.5-5.5 thioproperazine bound to the enzyme-substrate complex and caused a nticompetitive inhibition of peroxidase. At pH>5.5 sequential substrate oxidation with preferential thioproperazine conversion occurred. In the range of pH from 4.5 to 7.5 triftazine did not influence ODN oxidation. Source

Rogozhin V.V.,Yakutsk State Agricultural Academy | Peretolchin D.V.,Yakutsk State Agricultural Academy
Moscow University Chemistry Bulletin | Year: 2010

The study-state kinetics of individual and cooxidation of ferrocyanide and dihydroquercetin catalyzed by horseradish peroxidase is studied. It is shown that ferrocyanide and dihydroquercetin are slowly oxidized substrata peroxidase. In an interval of pH 4.5-8.0, sizes kcat and Km for these substrata peroxidase are certain. In reactions of cooxidation substrata, it was revealed that, at pH 4.5-7.0, dihydroquercetin accelerated oxidation ferrocyanide. At pH 7.5 oxidation only dihydroquercetin was observed. Mechanisms of reactions of combined oxidation ferrocyanide and dihydroquercetin are offered. © 2010 Allerton Press, Inc. Source

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