Limited Proteolysis of Horse Heart Cytochrome c
نویسندگان
چکیده
منابع مشابه
The action of cyanogen bromide on horse-heart cytochrome c and horse-heart myoglobin.
1. The effects of cyanogen bromide on horse-heart cytochrome c and horse-heart myoglobin have been investigated. Cytochrome c yielded four fragments, of which two were haemopeptides. The two colourless peptides had amino acid compositions corresponding to those that are expected, on the basis of the sequence proposed for horse-heart cytochrome c by Margoliash, Smith, Kreil & Tuppy (1961), from ...
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...
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 کاملComparative solvent perturbation of horse heart cytochrome c and Rhodospirillum rubrum cytochrome c2.
The extent of exposure of heme to solvent in horse heart cytochrome c and Rhodospirillum rubrum c2 was investigated to determine whether a correlation exists between the properties of these oxidation-reduction proteins and their heme environments. Solvent perturbation absorption difference spectra were measured using ethylene glycol, glycerol, and sucrose at concentrations between 0 and 30%. Cy...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1971
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1971.tb01407.x