Multiple Molecular Forms of Bovine Heart Cytochrome c

Multiple molecular forms of bovine heart cytochrome c. V. A comparative study of their physicochemical properties and their reactions in biological systems.

The differences in the physicochemical and electron transfer properties of the multiple forms of bovine heart cytochrome c, Cy I to Cy IV, provide a means of correlating substitutions of aspartyl or glutamyl residues for asparaginyl or glutaminyl residues in the polypeptide chain with the conformation of this heme protein, as well as a new aspect in the study of the relation between its structu...

The amino acid sequence of bovine heart cytochrome c.

Multiple Forms of Cytochrome c in the Rat

1. The heterogeneity of cytochrome c obtained in the monomeric form from different organs of rat was studied. Disc electrophoresis on polyacrylamide gel ievealed the presence of four forms in heart muscle, liver, and kidney. In the kidney, the mean percentage distribution was Cy I 86.2 %, Cy II S.O%, Cy III 4.2%, and Cy IV 1.6%. 2. The rate at which radioactive iron (SYFe) is incorporated into ...

Properties of Bovine Heart Mitochondrial Cytochrome

A large-scale preparation of the two-subunit protein complex (QPs) that converts succinate dehydrogenase into succinate-ubiquinone reductase from cytochrome 6-c, particles is achieved by a procedure involving Triton X100 solubilization and calcium phosphate column chromatography at different pH values. The isolated two-subunit QPs contains 25 nmol of cytochrome basofmg of protein and is able to...

Quantitative reevaluation of the redox active sites of crystalline bovine heart cytochrome c oxidase.

Approximately 30% of the iron contained in a bovine heart cytochrome c oxidase preparation was removed by crystallization, giving a molecular extinction coefficient 1.25-1.4 times higher than those reported thus far. Six electron equivalents provided by dithionite were required for complete reduction of the crystalline cytochrome c oxidase preparation. The fully reduced enzyme was oxidized with...