Hydration-State Change of Horse Heart Cytochrome c Corresponding to Trifluoroacetic-Acid-Induced Unfolding

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Amino 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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Multiple kinetic intermediates accumulate during the unfolding of horse cytochrome c in the oxidized state.

The unfolding kinetics of horse cytochrome c in the oxidized state has been studied at 10, 22, and 34 degreesC as a function of guanidine hydrochloride (GdnHCl) concentration. Rapid (millisecond) measurements of far-UV circular dichroism (CD) as well as fluorescence quenching due to tryptophan to heme excitation energy transfer have been used to monitor the unfolding process. At 10 degreesC, th...

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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 ...

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Spectral 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 ...

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Interconversion 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...

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ژورنال

عنوان ژورنال: Biophysical Journal

سال: 2013

ISSN: 0006-3495

DOI: 10.1016/j.bpj.2012.11.3825