{'fraction_non_alphanumeric': 0.016798418972332016, 'fraction_numerical': 0.008893280632411068, 'mean_word_length': 5.33125, '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}}
Metabolism of ethylmorphine and aniline in human fetal liver

The oxidative demethylation of ethylmorphine and the hydroxylation of aniline were studied in different centrifugal fractions of the human fetal liver. The rates of metabolism of ethylmorphine and aniline per milligram of protein in the microsomal fraction were 35 and 40 per cent, respectively, of the corresponding values in human adult liver microsomes. The metabolic activity in the different centrifugal fractions, expressed as per cent of total, corresponded to the activities of microsomal marker enzymes in the same fractions (see the preceding paper in this issue). The rate of demethylation of ethylmorphine per gram of human fetal liver was somewhat lower than that in human adult liver, while the rate of aniline hydroxylation was greater. The apparent Km value for ethylmorphine demethylation was 1 to 2 · 10‐5M. Both metabolic pathways appear to be nicotinamide adenine dinucleotide phosphate reduced (NADPH) dependent and CO sensitive.