نتایج جستجو برای: peroxidase

تعداد نتایج: 30160  

Journal: :The Journal of biological chemistry 1979
W D Hewson L P Hager

Horseradish peroxidase and chlorite, NaC102, are able to catalyze chlorination of monochlorodimedone to form dichlorodimedone. Catalytic amounts of horseradish peroxidase act to disproportionate chlorite forming chlorine dioxide and chloride ion. The chlorine dioxide thus formed is responsible for the chlorination of monochlorodimedone. It was previously thought (Chiang, R., Rand-Meir, T., Maki...

2005
Shigeru SHIGEOKA Yoshihisa NAKANO

Euglena gracilis was found to contain a peroxidase that specifically requires L-ascorbic acid as the natural electron donor in the cytosol. The presence of an oxidation-reduction system metabolizing L-ascorbic acid was demonstrated in Euglena cells. Oxidation of L-ascorbic acid by the peroxidase, and the absence of ascorbic acid oxidase activity, suggests that the system functions to remove H20...

Journal: :The Journal of biological chemistry 1977
M Y Wang B M Hoffman P F Hollenberg

Horseradish peroxidase can be reconstituted with cobalt porphyrin to give a cobaltic holoenzyme having physicochemical properties quite similar to those of the native ferric protein. The cobaltic protein (Co3+HRP) can be reduced to the cobaltous form (CoHRP), the analogue of ferroperoxidase and the reduced cobalt protein can bind O2 to form an analogue of oxyferroperoxidase (Compound III). Sinc...

2003

Recent studies have indicated that peroxidase might function in the biological synthesis of thyroxine by the thyroid gland. Johnson and Tewkesbury (1) believed that thyroxine might be formed by the oxidative coupling of 2 molecules of diiodotyrosine. Westerfeld and Lowe (2) studied the oxidative condensation of p-cresol by hydrogen peroxide and peroxidase and suggested that peroxidase might be ...

Journal: :Qeios 2023

In this work, unmodified silver nanoparticles were synthesized by a simple and cost-efficient method then characterized TEM imaging UV-Vis. spectroscopy. Thereafter, their nanozymatic activity was investigated catalyzing the oxidation of 3,3’,5,5’-tetramethyl-benzidine (TMB) as standard peroxidase substrate. The results exhibited specific high 5.4 µM min-1 for as-prepared nanoparticles. Afterwa...

Journal: :Applied and environmental microbiology 1996
D K Mercer M Iqbal P Miller A J McCarthy

A diverse collection of actinomycete strains were screened for production of extracellular peroxidase activity by adapting a chemiluminescence analysis system developed for horseradish peroxidase-based enzyme-linked immunosorbent assay. Extracellular peroxidase activity was found to be common but quantitatively variable, and this rapid and sensitive screening system permitted identification of ...

Journal: :Plant physiology 1978
R Borchert

The time course and spatial distribution of wound-induced activities of phenylalanine ammonia-lyase and peroxidase were determined to establish correlations between molecular and cellular aspects of the wound-induced pattern of cell differentiation in potato (Solanum tuberosum L.) tissue. A high correlation between peroxidase activity and suberization was observed. Peroxidase activity increased...

Journal: :Glycobiology 1998
I B Wilson J E Harthill N P Mullin D A Ashford F Altmann

Carbohydrates have been suggested to account for some IgE cross-reactions between various plant, insect, and mollusk extracts, while some IgG antibodies have been successfully raised against plant glycoproteins. A rat monoclonal antibody raised against elderberry abscission tissue (YZ1/2.23) and rabbit polyclonal antiserum against horseradish peroxidase were screened for reactivity in enzyme-li...

Journal: :The Journal of biological chemistry 1974
P F Hollenberg T Rand-Meir L P Hager

Chloroperoxidase and horseradish peroxidase use NaClOz as both the oxidant and the halogen donor for the peroxidative chlorination of monochlorodimedone. Previous studies have shown that both horseradish peroxidase and chloroperoxidase can catalyze iodination reactions with hydrogen peroxide as the oxidant; however, only chloroperoxidase catalyzes chlorination reactions under these conditions. ...

Journal: :The Biochemical journal 1977
P Agrawal M M Laloraya

The lutropin-induced depletion of ascorbate in corpora lutea of albino-rat ovary is shown to be associated with the induction of peroxidase in corpora lutea. An inverse relationship between ascorbate depletion and peroxidase activity was established in a time-course study with lutropin. Analyses made at different phases of the reproductive cycle are in accord with this relationship. It is sugge...

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