{'fraction_non_alphanumeric': 0.015065913370998116, 'fraction_numerical': 0.005649717514124294, 'mean_word_length': 5.487804878048781, '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}}
A kinetic evaluation of monoamine oxidase activity in rat liver mitochondrial outer membranes.

1. A preparation of mitochondrial outer membranes from rat liver can be shown to contain two kinetically distinct monoamine oxidase activities. These activities are distinguishable by their different sensitivities to the irreversible inhibitor clorgyline, and by the effect of the reversible inhibitors benzyl cyanide and 4-cyanophenol. 2. The substrate specificities of the preparation and the two enzyme species have been elucidated.