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Abstract

Cytochrome c of mammalian (porcine, horsy and bovine) heart muscle was isolated and highly purified by the repeated chromatography on a column of "column-lite" a synthesized magnesium aluminosilicate of particle sizes from 30 to 60 meshes. Cytochrome c was adsorbed on the ion-exchanger at pH 7.4 and was eluted by around 5.0% ammonium sulfate solution of pH 7.4. Three time-repetition of the chromatography resulted in isolation of nearly pure cytochrome c. The purity was shown by the absorption spectra of the exidized and reduced form, gel filtration on Sephadex G-75 and electrophoresis on a cellulose acetate sheet and acrylamide gel.