Biochemical basis for the resistance of guinea-pig and monkey to the carcinogenic effects of arylamines and arylamides.
作者： C. Razzouk , M. Mercier , M. Roberfroid
DOI: 10.3109/00498258009033791
关键词: Enzyme 、 Methylcholanthrene 、 Biochemistry 、 Hydroxylation 、 Metabolite 、 2-Acetylaminofluorene 、 Allosteric regulation 、 Carcinogen 、 Microsome 、 Biology
摘要: 1. Ag.l.c. assay for N-hydroxy-2-acetamidofluorene has been modified to measure both and N-hydroxy-2-aminofluorene. 2. Like guinea-pig, monkey N-hydroxylates 2-aminofluorene 2-acetamido-fluorene. The N-hydroxy metabolites are rapidly further metabolized even in the presence of inhibitors deacetylase. exact nature this metabolism is still unknown. Preliminary evidence indicates that, at least 7-hydroxy-2-acetamidofluorene may be a metabolite N-hydroxy-2-acetmidofluorene. 3. 3-Methylcholanthrene, 7,8-benzoflavone miconazole, which have shown inhibit guinea-pig liver microsomal N-hydroxylase, do not significantly enzyme. 4. 2-Acetamidofluorene, inhibits N-hydroxylation vitro, activates enzyme from liver. This activation, dose-dependent, appears allosteric. 5. Both more efficient N-hydroxylating than 2-acetamidofluorene. affinity (in term apparent KM) 4 times greater
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