Cytochrome c from Schizosaccharomyces pombe

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Abstract
Cytochrome c from the fission yeast S. pombe was purified. Its chromatographic and spectral properties are reported and compared to those of iso-1-cytochrome c from baker''s yeast; the amino-acid composition is described. S. pombe cytochrome c has a much lower affinity for Amberlite IRP64 than Saccharomyces S cerevisiae iso-1-cytochrome c. Its .alpha. absorption band splits into 3 maxima (c.alpha.1, c.alpha.2 and c.alpha.3) at -190.degree. C; this is unusual in yeasts, as shown by the low-temperature whole-cell absorption spectra which were examined in various yeast genera, species and strains. A minor component can be separated by Amberlite chromatography. It exhibits the same low-temperature splitting of the .alpha. absorption band as the main fraction and it has a similar amino-acid composition with a notable exception: it is an unmethylated form of the cytochrome.