Abstract
A c-type cytochrome was highly purified from nuclei of calf thymus gland by deoxyribonuclease digestion, salt extraction, ammonium sulfate fractionation, and Amberlite CG-50 column chromatography. Cytochrome c was also purified from calf thymus mitochondria by the same procedure. The two cytochrome c preparations were found to be indistinguishable from each other in spectral properties, redox potential, electrophoretic behavior, reactivities, amino acid composition and peptide map pattern. It was concluded that the thymocyte contains the same species of cytochrome c in both the nucleus and mitochondria.

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