Amino Acid Composition of Horse Heart Cytochrome c

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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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Isolation and amino acid composition of chymotryptic peptides from horse heart cytochrome c.

Mammalian cytochrome c is a protein of low molecular weight (approximately 12,500) (l-3) containing one heme per mole of protein. Through the efforts of many investigators, our knowledge of its biological function and over-all physicochemical properties is well documented (see reviews by Paul (4), Keilin and Slater (5), and George and Lyster (6)) ; however, there is relatively little informatio...

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Amino acid sequence of chymotryptic peptides from horse heart cytochrome c.

The preparation, purification, and amino acid composition of peptides obtained from a chymotryptic digest of horse heart cytochrome c have been described in the preceding paper (1). The present work is concerned with the determination of the amino acid sequence of these peptides, which account for the complete composition of the protein. Combining the results of the present work with those of K...

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Amino acid sequence of chicken heart cytochrome c.

The complete amino acid sequence of chicken heart cytochrome c has been established. This primary structure is typically that of a “mammalian-type” cytochrome c showing the characteristic groupings of hydrophobic and basic residues, and, like the other cytochromes c from vertebrate species, has an acetylated amino-terminal residue. Chicken heart cytochrome c differs from the horse, beef, human,...

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Amino acid sequence of rhesus monkey heart cytochrome c.

Elucidation of the primary structures of the cytochromes c from several species of mammals (l-5), tuna fish (6), chicken (3), and yeast (7) has provided considerable insight into the evolution of cytochrome c and the structural features which may potentiate its biological activity. These topics and further implications of the knowledge derived from study of the comparative structures of cytochr...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1962

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(19)63411-3