Results 211 to 220 of about 33,389 (238)
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Partial purification and properties of catechol oxidases in grapes
Phytochemistry, 1971Abstract Grapes contain a high level of catechol oxidase activity. The enzyme is located in a particulate fraction of the cell, apparently in the plastids. It resembles catechol oxidases from other fruits in many aspects but differs in its relatively high activity towards caffeic and p-hydroxycinnamic acids and in its high affinity towards the latter.
E. Harel, A.M. Mayer
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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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Assay of catechol oxidase—a critical comparison of methods
Phytochemistry, 1966Abstract Manometric, polarographic, chronometric and spectrophotometric methods for the determination of catechol oxidase activity were critically compared. Where possible, product formation, disappearance of substrate and ratios between oxygen uptake and substrate disappearance were determined.
A.M. Mayer, E. Harel, R. Ben-Shaul
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Limitations of the quantitative cytochemical assay of catechol oxidase in melanoma cells
The Histochemical Journal, 1988The cytochemical quantification of catechol oxidase activity in fixed B16 melanoma cells was investigated using dopa as the substrate. Inhibitors showed that peroxidases do not significantly interfere. The kinetics of melanin formation were studied initially in solution with purified catechol oxidase.
A C, Croce +4 more
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Crystal structure of a plant catechol oxidase containing a dicopper center
Nature Structural Biology, 1998Catechol oxidases are ubiquitous plant enzymes containing a dinuclear copper center. In the wound-response mechanism of the plant they catalyze the oxidation of a broad range of ortho-diphenols to the corresponding o-quinones coupled with the reduction of oxygen to water. The crystal structures of the enzyme from sweet potato in the resting dicupric Cu(
T, Klabunde +3 more
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Impressive promiscuous biomimetic models of ascorbate, amine, and catechol oxidases
Journal of Inorganic BiochemistryCopper metalloenzymes ascorbate oxidase (AOase), amine oxidase (AmOase), and catechol oxidase (COase) possess copper(II) sites of coordination, which are trimeric, homodimeric, and dimeric, respectively. Two newly mononuclear copper(II) complexes, namely, [Cu(L)(bpy)](ClO4) (1) and [Cu(L)(phen)](ClO4) (2) where HL = Schiff base, have been synthesized ...
Balasubramaniam, Selvakumaran +4 more
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The Intracellular Location of Catechol Oxidase
Annals of Botany, 1979I. SHOMER +3 more
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