Results 151 to 160 of about 20,124 (183)

Platinum Nanoparticles: Efficient and Stable Catechol Oxidase Mimetics

ACS Applied Materials & Interfaces, 2015
Although enzyme-like nanomaterials have been extensively investigated over the past decade, most research has focused on the peroxidase-like, catalase-like, or SOD-like activity of these nanomaterials. Identifying nanomaterials having oxidase-like activities has received less attention. In this study, we demonstrate that platinum nanoparticles (Pt NPs)
Yi, Liu, Haohao, Wu, Yu, Chong, Wayne G, Wamer, Qingsu, Xia, Lining, Cai, Zhihong, Nie, Peter P, Fu, Jun-Jie, Yin   +8 more
openaire   +2 more sources

Catechol oxidase of red delicious apple peel

Phytochemistry, 1972
Abstract Catechol oxidase has been solubilized from the particulate fraction of apple peel using Triton X-100, dialysis and butanol extraction. The partially purified enzyme retained activity during lyophilization in the presence of mercaptobenzothiazole. The substrate specificity and pH optima of the enzyme are reported.
David A. Stelzig, S. Akhtar, S. Ribeiro
openaire   +1 more source

Synthetic models of the active site of catechol oxidase: mechanistic studies

Chemical Society Reviews, 2006
AbstractChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 200 leading journals. To access a ChemInform Abstract, please click on HTML or PDF.
Koval, Iryna, Gamez, Patrick, Belle, Catherine, Selmeczi, Katalin, Reedijk, Jan   +4 more
openaire   +3 more sources

Partial purification and properties of catechol oxidases in grapes

Phytochemistry, 1971
Abstract 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
openaire   +1 more source

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

Multiple forms of Vitis vinifera catechol oxidase

Phytochemistry, 1973
Abstract Grape catechol oxidase shows multiple forms upon ion exchange chromatography, acrylamide gel electrophoresis and gel filtration. Conversion of some bands into others, which occurs during isolation and storage, is enhanced by dilution and by treatment with urea or acid pH.
Eitan Harel, Alfred M. Mayer, Eliakim Lehman   +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, E. Harel, E. Lehman, A.M. Mayer   +3 more
openaire   +1 more source

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
exaly   +2 more sources

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, Sarah M. Narehood, Yiying Li, Mauro Gascón, Alexander M. Hoffnagle, Angela A. Shiau, Manny Semonis, Michael T. Green, R. David Britt, F. Akif Tezcan   +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, G, Bottiroli, E, Prosperi, R, Supino, P J, Stoward   +4 more
openaire   +2 more sources