Multiple components in horse-radish peroxidase

ABSORPTION OF THE HORSE-RADISH PEROXIDASE IN THE SMALL INTESTINE OF CmCKEN

Holman J.: Absorption of the Horse-radish Peroxidase in the Small Intestine of Chicken. Acta vet. Brno, 47, 1978: 3-6. Localization of the horse-radish peroxidase was studied in the epithelium and stroma of the small intestitlal villi in the chic:, aged 37 days. The enzyme (molecular weight 40.000) was injected into the ligated jejunal loop. Its enteral absorption was shown to proceed via the s...

Compounds I of Catalase and Horse Radish Peroxidase : 7 r - Cation Radicals

Two-electron oxidation of cobaltous actaethylporphyrin [Co(II)(Et).P] yields a stable ...... cation radical [Co(III)(Et)8P]'+·, the optical spectrum of which exhibits spectral changes dependent upon the nature of the counterion. COInparison of these spectra with those of Compounds I of horseradish peroxidase and catalase leads us to propose that these Compounds I contain a 7r-cation radical of ...

Compounds I of catalase and horse radish peroxidase: pi-cation radicals.

Two-electron oxidation of cobaltous octaethylporphyrin [Co(II)(Et)(8)P] yields a stable pi-cation radical [Co(III)(Et)(8)P](2+.), the optical spectrum of which exhibits spectral changes dependent upon the nature of the counterion. Comparison of these spectra with those of Compounds I of horseradish peroxidase and catalase leads us to propose that these Compounds I contain a pi-cation radical of...

Purification of horse-radish peroxidase and comparison of its properties with those of catalase and methaemoglobin.

Aerobic oxidation of p-hydroquinone by horse radish peroxidase in the presence of a thiol and MnCl2.

In the presence of MnCl2 and a thiol (glutathione, cysteine, 2-nitro-5-thiobenzoic acid) horse radish peroxidase oxidizes p-hydroquinone to p-benzoquinone which in turn immediately adds the thiol present yielding 2-S-substituted p-hydroquinone.