Results 241 to 250 of about 34,133 (279)
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Isoelectric point changes in Vitis vinifera catechol oxidase
Phytochemistry, 1974Abstract A comparison between electrophoretic and isoelectric focussing patterns of grape catechol oxidase is reported.
M. Dubernet, null Ribéreau-Gayon
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Stokes' radius changes of solubilized grape catechol oxidase
Phytochemistry, 1975Abstract 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
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Enzymatic dynamics of catechol oxidase from Gastrolina depressa
Pesticide Biochemistry and Physiology, 2010Abstract 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
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Tea catechol oxidase: Isolation, purification and kinetic characterization
Phytochemistry, 1973Abstract 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
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Phenylhydrazine, a specific irreversible inhibitor of catechol oxidase
Phytochemistry, 1971Abstract 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
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ACS Applied Materials & Interfaces, 2017
Oxidases are found to play a growing role in providing functional chemistry to marine adhesives for the permanent attachment of macrofouling organisms. Here, we demonstrate active peroxidase and lysyl oxidase enzymes in the adhesive layer of adult Amphibalanus amphitrite barnacles through live staining, proteomic analysis, and competitive enzyme assays
Christopher R. So +14 more
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Oxidases are found to play a growing role in providing functional chemistry to marine adhesives for the permanent attachment of macrofouling organisms. Here, we demonstrate active peroxidase and lysyl oxidase enzymes in the adhesive layer of adult Amphibalanus amphitrite barnacles through live staining, proteomic analysis, and competitive enzyme assays
Christopher R. So +14 more
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Catechol oxidase from green olives: Properties and partial purification
Phytochemistry, 1977Abstract 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
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Reaction mechanism of grape catechol oxidase—a kinetic study
Phytochemistry, 1976Abstract The initial velocity of the oxidation of 4-methylcatechol by grape catechol oxidase was determined. The kinetic analysis indicates that first there is random binding of an oxygen and a 4-methylcatechol molecule to the enzyme. Then one product molecule is released prior to the binding of second 4-methylcatechol molecule which is followed by ...
H.R. Lerner, A.M. Mayer
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Isolation and characterization of catechol oxidase from Solanum melongena
Phytochemistry, 1980Abstract Catechol oxidase was distributed in soluble and particulate fractions of Solanum melongena . The purified preparation appears to be homogeneous by polyacrylamide gel electrophoresis. The enzyme shows two pH maxima—with catechol, 6.5 and 7.5; and with dopa, 6.5 and 7.9. The latent form of the enzyme does not occur in S. melongena .
Rakesh C. Sharma, Rashid Ali
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Catechol oxidase: Enzymic liberation from sugar beet chloroplasts
Phytochemistry, 1966Abstract Catechol oxidase present in isolated sugar beet chloroplasts is activated by means of proteolytic enzymes. The most effective treatment is a combination of trypsin and carboxypeptidase a. This gives a fourfold activation and releases the catechol oxidase from its bound form.
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