Results 181 to 190 of about 306,357 (240)
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Zero‐Order Catechol Oxidase Activity by a Mononuclear Manganese(III) Complex Showing High Turnover Comparable to Catechol Oxidase Enzyme

ChemCatChem, 2013
Enzymatic mimics are designed by using small molecules to impart insight into the mechanistic pathways of the enzymes and to generate catalysts that could be as efficient as the enzyme itself. Among the copper-based polyphenol oxidase enzymes, the copper(II)-containing enzyme catechol oxidase catalyses exclusively the oxidation of ortho-diphenols to ...
Suman Kr Dey, Arindam Mukherjee
openaire   +1 more source

Ag-doped CdO nanocatalysts: Preparation, characterization and catechol oxidase activity

Journal of Molecular Structure, 2018
Silver doped cadmium oxide (Ag/CdO) nanoparticles with an average size of 41 nm have been successfully synthesized via thermal decomposition and liquid impregnation technique.
M. El-Kemary   +2 more
semanticscholar   +1 more source

Evidence for conformational changes in grape catechol oxidase

Phytochemistry, 1972
Abstract A rapid, 4–10-fold, activation of grape catechol oxidase by a short exposure to acid pH or urea is demonstrated. Activation was either reversible or irreversible, depending on length and type of treatment. The change in activity of the enzyme is due primarily to an increase in V max , while the affinity for 4-methylcatechol decreases and ...
H.R. Lerner, A.M. Mayer, E. Harel
openaire   +1 more source

Isoelectric point changes in Vitis vinifera catechol oxidase

Phytochemistry, 1974
Abstract A comparison between electrophoretic and isoelectric focussing patterns of grape catechol oxidase is reported.
M. Dubernet, null Ribéreau-Gayon
openaire   +1 more source

Stokes' radius changes of solubilized grape catechol oxidase

Phytochemistry, 1975
Abstract The Stokes' radius of grape catechol oxidase was determined at pH 7·0 and during its reversible and irreversible activation at pH 5·0. The results are consistent with the view that the activation is due to a conformational change in the enzyme.
H.R. Lerner, A.M. Mayer
openaire   +1 more source

Enzymatic dynamics of catechol oxidase from Gastrolina depressa

Pesticide Biochemistry and Physiology, 2010
Abstract Properties of the phenoloxidase (PO) from adult of Gastrolina depressa Baly (Coleoptera: Chrysomelidae) as well as effects of some metal ions and inhibitors on the activity of PO purified by (NH 4 ) 2 SO 4 were determined. The optimal pH and temperature of the enzyme for the oxidation of catechol were determined to be at pH 7.5 and at 40 °
Yan Zhao   +4 more
openaire   +1 more source

Tea catechol oxidase: Isolation, purification and kinetic characterization

Phytochemistry, 1973
Abstract Cathechol oxidase extracted from tea leaves was purified over 200-fold, using isoelectric focusing. The purified catechol oxidase was free of peroxidase and flavanol gallate esterase activities. Further, this enzyme was shown to have optimum activity near pH 5·7 and a Km of 2·3 × 10−3 M (at 25°) for (−)-epigallocatechin gallate. The purified
Philip Coggon   +2 more
openaire   +1 more source

Phenylhydrazine, a specific irreversible inhibitor of catechol oxidase

Phytochemistry, 1971
Abstract Phenylhydrazine is shown to specifically inhibit a number of catechol oxidases from plant tissues. A laccase-like enzyme from peaches is not inhibited while ascorbic oxidase is only partly inhibited by relatively high concentrations of the inhibitor.
H.R. Lerner   +3 more
openaire   +1 more source

Catechol oxidase from green olives: Properties and partial purification

Phytochemistry, 1977
Abstract Catechol oxidase was extracted from an acetone powder prepared from green olive. The enzyme was purified 240-fold by ammonium sulphate fractionation followed by ion exchange chromatography and gel filtration. The enzyme was characterized by substrate specificity and response to inhibitors.
Noach Ben-Shalom   +3 more
openaire   +1 more source

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