Human Heart Cytochrome c

Running title: Novel Human Cytochrome c Targets

Comparative biochemical studies. I. Purification and crystallization of human heart cytochrome c.

In recent years, numerous human enzymes and proteins have been crystallized and some studies have been made to determine physicochemical differences between those from human and from other animal species (l-3). Some of these studies have indicated that there are species differences. It was of interest to extend these studies to other proteins. Cytochrome c was chosen in the present study becaus...

A 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,...

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,...

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...