منابع مشابه
Topographic Antigenic Determinants on Cytochrome c IMMUNOADSORBENT SEPARATION OF THE RABBIT ANTIBODY POPULATIONS DIRECTED AGAINST HORSE CYTOCHROME c*
Seven populations of site-specific antibodies were isolated from each of three sera of rabbits immunized against glutaraldehyde-polymerized horse cytochrome c. The antibodies were separated using an immunoadsorption scheme which employed the following cytochromes c: horse, beef, guanaco, rabbit, mouse testicular, pigeon, and the cyanogen-bromide cleaved fragment of the rabbit protein containing...
متن کاملA triphosphopyridine nucleotide-cytochrome c reductase from heart muscle.
Extensive studies by numerous workers have served to characterize the reduced diphosphopyridine nucleotide and succinic oxidase systems as important enzymatic pathways in the terminal respiratory chain of mammalian tissue [see reviews by Chance (1) and Slater (2)]. These systems have been shown to consist of an integrated complex of components including flavins, various cytochromes, metal ions,...
متن کاملAmino 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,...
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 کاملAmino 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: 1966
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)96843-2