Results 171 to 180 of about 19,268 (196)
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Assay of catechol oxidase—a critical comparison of methods

Phytochemistry, 1966
Abstract 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
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

Computational Design of a Highly Stable Dicopper Catechol Oxidase

Journal of the American Chemical Society
Type 3 (T3) Cu proteins play essential roles in binding and activating molecular oxygen (O2) and are prevalent across all domains of life. Despite sharing the same coordination motif, T3 Cu proteins display divergent functions: hemocyanin transports O2, while tyrosinase catalyzes the hydroxylation of monophenols and the subsequent oxidation of ...
Vanessa H. Eng   +9 more
openaire   +2 more sources

Limitations of the quantitative cytochemical assay of catechol oxidase in melanoma cells

The Histochemical Journal, 1988
The 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
openaire   +2 more sources

Crystal structure of a plant catechol oxidase containing a dicopper center

Nature Structural Biology, 1998
Catechol 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
openaire   +2 more sources

Catechol Oxidase in Tissue 4

Journal of Experimental Botany, 1977
RUTH VOLK   +3 more
openaire   +1 more source

Catechol oxidase

1994
D. Schomburg, M. Salzmann, D. Stephan
openaire   +1 more source

The Intracellular Location of Catechol Oxidase

Annals of Botany, 1979
I. SHOMER   +3 more
openaire   +1 more source

Catechol Oxidase Activity in Grapes and Wine

American Journal of Enology and Viticulture, 1978
M. Kidron, E. Harel, A. M. Mayer
openaire   +1 more source

Catechol oxidase (dimerizing)

1995
Dietmar Schomburg, Dörte Stephan
openaire   +1 more source

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