{'fraction_non_alphanumeric': 0.027314112291350532, 'fraction_numerical': 0.027314112291350532, 'mean_word_length': 5.875, 'pattern_counts': {'":': 0, '<': 0, '<?xml version=': 0, '>': 0, 'https://': 0, 'lorem ipsum': 0, 'www.': 0, 'xml': 0}, 'pii_count': 0, 'substrings_counts': 0, 'word_list_counts': {'cursed_substrings.json': 0, 'profanity_word_list.json': 0, 'sexual_word_list.json': 0, 'zh_pornsignals.json': 0}}
Characterization of solubilized cytochrome P-450.

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 NO2- 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 b5 and significant amounts of ferricyanide reductase and NADPH oxidase activity.