Crystalline cytochrome P-450cam, the oxygen- and sub- strate-reactive component of a selective methylene 5-exo-hydroxylase, has been prepared from camphor-induced cells of Pseudomonas putida, strain PpG786, by two similar procedures. The first involved autolysis, DEAE-cellulose chromatography, ammonium sulfate fractionation, Sephadex G-75 filtration, calcium phosphate gel chromatography, and crystallization from ammonium sulfate. Procedure II involved Bio-Gel P-150 filtration, DEAE-Sephadex and DEAE-cellulose chromatography, and ammonium sulfate fractionalization. The purified cytochrome P-450cam has a molecular weight in the range of 44,000 to 46,000, depending upon the method of determination. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis indicated that the protein moiety is composed of a single polypeptide.
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Yu et al. (1974) studied this question.
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