Abstract
Rat hepatic microsomal cytochrome b5 was purified to homogeneity by solubilization with the detergent Lubrol 12-A9 and chromatography on Fractogel TSK DEAE-650(S). The protein was obtained in high yield (52-87%) in 8 h, and only 1 polypeptide band, of MW 16,600, was visible after sodium dodecyl sulfate/polyacrylamide-gel electrophoresis.