Abstract
Cytochrome b of R. sphaeroides R-26 has been purified from the isolated cytochrome b-c1 complex to homogeneity. The purification procedure involves Triton X-100 and urea solubilization, calcium phosphate column chromatography at different pH values, and ammonium sulfate fractionation. The purified protein contains 23 nmol heme per mg protein and has an apparent molecular weight of 43,000, as determined by sodium dodecylsulfate polyacrylamide gel electrophoresis. The spectral characteristics of purified cytochrome b are similar to those of cytochrome b in the active cytochrome b-c1 complex but with a lower absorbance. The amino acid composition has been determined and compared with cytochrome b purified from other sources.
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