Cocrystals of yeast cytochrome c peroxidase and horse heart cytochrome c.
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چکیده
منابع مشابه
Peroxidase activity enhancement of horse cytochrome c by dimerization.
The peroxidase activity of horse cytochrome c was enhanced by its dimerization, where its Compound III (oxy-form) and Compound I (oxoferryl porphyrin π-cation radical) species were detected in the reactions with hydrogen peroxide and meta-chloroperbenzoic acid, respectively. These results show that oligomeric cytochrome c can contribute as a proapoptotic conformer by the increased peroxidase ac...
متن کاملInterconversion of horse heart cytochrome C monomer and polymers.
When preparations of cytochrome c from mammalian species are chromatographed on columns of weak cation exchange agents, more than one chromatographic species can be obtained (1, 2). Only one of these fractions, that elutcd from the polycarboxylic resin Amberlite IRC-50 (Rohm and Hnas Company) at sodium or ammonium ion concentrations of 0.22 to 0.25 equivalent per liter (2, 3), can be considered...
متن کاملStudies on Cytochrome c Peroxidase
Apoproteins of cytochrome c peroxidase, horseradish peroxidase, and sperm whale myoglobin were recombined with manganese complexes of proto-, hemato-, meso-, and deuteroporphyrins to form manganese porphyrin-protein complexes. These complexes were purified by column chromatography. All the manganese porphyrin-containing cytochrome c peroxidases were crystallized. Light absorption maxima of mang...
متن کاملSpectral studies of horse heart porphyrin cytochrome c.
Removal of the heme iron from cytochrome c to generate porphyrin cytochrome c relieves the quenching of porphyrin fluorescence and enhances the fluorescence of the single tryptophan residue and the 4 tyrosine residues. The intensity of the porphyrin fluorescence is not perturbed by denaturation of the protein at neutral pH using either urea or guanidine hydrochloride. However, the amplitude of ...
متن کاملAmino acid composition of horse heart cytochrome c.
As the first step in the study of the amino acid sequence of horse heart cytochrome c, it was essential to establish the exact composition of the protein. Although the molecular weight is low (approximately 12,000) (1) and the protein contains less than 110 amino acid residues per mole, analyses by three diierent laboratories (2-4) have not yielded strictly concordant results. These analyses ar...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1987
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)47874-x