Abstract
Cytochrome c 1 of photosynthetic bacterium R . sphaeroides R-26 has been purified from isolated cytochrome b - c 1 complex to a single polypeptide, using a procedure involving Triton X-100 and urea solubilization, calcium phosphate column chromatography and ammonium sulfate fractionation. The purified protein contains 30 nmoles heme per mg protein and has an apparent molecular weight of 30,000, as determined by sodium dodecylsulfate polyacrylamide gel electrophoresis. Bacterial cytochrome c 1 is soluble in aqueous solution in the absence of detergent and has spectral characteristics similar to mammalian cytochrome c 1 . The amino acid compositions of these two proteins, however, are not comparable.
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