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Stereospecificity of horseradish peroxidase
Biological Chemistry, 2004We report here on the stereospecificity observed in the action of horseradish peroxidase (HRPC) on monophenol and diphenol substrates. Several enantiomers of monophenols and o-diphenols were assayed: L-tyrosinol, D-tyrosinol, L-tyrosine, DL-tyrosine, D-tyrosine, L-dopa, DL-dopa, D-dopa, L-alpha-methyldopa, DL-alpha-methyldopa, DL-adrenaline, D ...
José Tudela +6 more
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Looking for syringyl peroxidases
Trends in Plant Science, 2007Lignins are cell wall heteropolymers that arise from the peroxidase-mediated coupling of p-coumaryl, coniferyl and sinapyl alcohols. In gymnosperms, they are derived from coniferyl alcohol, whereas in angiosperms, lignins are derived from coniferyl and sinapyl alcohols. Thus, although it is frequently assumed that the chemical complexity of lignins has
Alfonso Ros Barceló +2 more
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Iodination by thyroid peroxidase
1984Publisher Summary The Iodination of tyrosyl moieties in thyroglobulin and other proteins is catalyzed by the thyroid peroxidase (TPO), an integral membrane, heme glycoprotein. Tyrosine and tyrosyl peptides can also be iodinated by TPO. The iodination reaction requires H 2 O 2 , I - , an enzyme-associated iodinating intermediate (TPO-I oxid ), and an ...
J T Neary, Farahe Maloof, Morris Soodak
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Peroxidase Oxidation of Phenols
Applied Biochemistry and Microbiology, 2004Partially purified preparations of horseradish peroxidase were able to catalyze the effective transformation of such phenol compounds as phenol, o-chlorophenol, 2,4,6-trichlorophenol, pentachlorophenol (giving rise to the formation of polymer products insoluble in water), resorcinol, and thymol (giving rise to the formation of low-molecular-weight ...
T. I. Davidenko +3 more
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1985
Catalase is the enzyme that catalyzes the decomposition of hydrogen peroxide to water and dioxygen. The usual sources of catalase are bovine liver and bovine erythrocytes. The enzyme exists as a 250,000–dalton tetramer with one heme per monomer. The complete amino acid sequence of the bovine liver enzyme is known (Schroeder et al., 1982) as well as ...
Damon L. Meyer, Llyod L. Ingraham
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Catalase is the enzyme that catalyzes the decomposition of hydrogen peroxide to water and dioxygen. The usual sources of catalase are bovine liver and bovine erythrocytes. The enzyme exists as a 250,000–dalton tetramer with one heme per monomer. The complete amino acid sequence of the bovine liver enzyme is known (Schroeder et al., 1982) as well as ...
Damon L. Meyer, Llyod L. Ingraham
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1975
We have seen how a protein can affect equilibrium constants (chapter 7). We now want to look at the more complex question of how the protein can affect the rates of reaction, and we shall examine the reactions of H2O2 with catalases and peroxidases. For a general introduction to these enzymes see the reviews by Nicholls and Schonbaum on catalases159 ...
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We have seen how a protein can affect equilibrium constants (chapter 7). We now want to look at the more complex question of how the protein can affect the rates of reaction, and we shall examine the reactions of H2O2 with catalases and peroxidases. For a general introduction to these enzymes see the reviews by Nicholls and Schonbaum on catalases159 ...
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Substrate Specificity of Peroxidase [PDF]
Science, 1955 Britton Chance, R. R. Fergusson
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