نتایج جستجو برای: horseradish peroxidase c

تعداد نتایج: 1081566  

Journal: :The Journal of biological chemistry 1981
G N La Mar J S de Ropp K M Smith K C Langry

Journal: :Biochimie 2008
Barry J Ryan Mary J O'Connell Ciarán O'Fágáin

The enzyme horseradish peroxidase has many uses in biotechnology but a stabilized derivative would have even wider applicability. To enhance thermal stability, we applied consensus mutagenesis (used successfully with other proteins) to recombinant horseradish peroxidase and generated five single-site mutants. Unexpectedly, these mutations had greater effects on steady-state kinetics than on the...

Journal: :The Journal of biological chemistry 1962
M MAZELIS

The most completely characterized peroxidase is horseradish peroxidase. It has been known for some time that this enzyme can act as an aerobic oxidase under certain conditions. Among the oxidative reactions catalyzed by this enzyme are the oxidation of dihydroxyfumaric acid (1, 2)) phenylacetaldehyde (3), phenylpyruvic acid (4)) dicarboxylic acids (5)) indoleacetic acid (6,7) reduced diphosphop...

Journal: :The Journal of Cell Biology 1979
K C Joseph A Stieber N K Gonatas

Cholera toxin (CT), covalently attached to horseradish peroxidase (HRP), is a specific cytochemical marker for GM1 ganglioside (GM1) and retains the ability of the native toxin to raise levels of cyclic AMP in avian erythrocytes. Using a cytochemical stain for HRP, we found that 9% of control cultured murine neuroblastoma cells bound cholera toxin-horseradish peroxidase conjugates (CT-HRP) on t...

2007
A. Bódalo J. L. Gómez J. Bastida M. F. Máximo

A comparative study of the two most widely used commercial peroxidases (E.C. 1.11.1.7) for removing 4-chlorophenol from aqueous industrial effluents is presented. Both the peroxidases tested, horseradish peroxidase (HRP) and soybean peroxidase (SBP), showed maximal removal efficiency in a neutral pH medium although they maintained more than 70 % of their activity in a pH range of between 6.0 an...

Journal: :The Journal of biological chemistry 1992
W J Chuang H E Van Wart

The nature of the porphyrin pi-cation radicals in the horseradish peroxidase and bovine liver catalase (BLC) compound I species have been investigated by studying their resonance Raman spectra. A variety of laser excitation and sample interrogation procedures have been employed in order to minimize previously documented problems arising from photoinduced conversions. With Soret band excitation,...

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