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Porcine liver microsomes were subjected to digitonin, n‐butanol and sonication treatment to solubilize cytochrome P‐450 and other mixed‐function oxidation components. The best preparation achieved with 2% digitonin gave characteristic P‐450, CN‐and NO 2 ‐ difference spectra. It was further purified by ammonium sulfate fractionation and column chromatography. Column chromatography resulted in the separation of cytochrome P‐450 subparticles from cytochrome P‐420 subparticles; both contained negligible quantities of cytochrome b 5 and significant amounts of ferricyanide reductase and NADPH oxidase activity.
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Koes et al. (1973) studied this question.
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