
doi: 10.1007/bf00485845
pmid: 10885
Aryl hydrocarbon hydroxylase and 16alpha-hydroxylase were examined in intact, cultured human lymphocytes. The two microsomal mixed-function oxygenases had different pH optima and showed competitive inhibition for enzyme induction and activity. Population distributions were lognormal for both enzymes, giving apparent evidence for polygenic control. Induced levels of AHH were slightly higher among first-order relatives of lung or colon cancer patients than in the control group. The correlation coefficient (r) for AHH and SAH coinducibility was -0.08, indicating no correlation and suggesting the absence of association between the two enzymes in man.
Lung Neoplasms, Estradiol, Hydrogen-Ion Concentration, Cytochrome P-450 CYP2C8, Isoenzymes, Kinetics, Enzyme Induction, Microsomes, Colonic Neoplasms, Steroid Hydroxylases, Humans, Aryl Hydrocarbon Hydroxylases, Lymphocytes, Cells, Cultured, Cytochrome P-450 CYP2C9, Methylcholanthrene
Lung Neoplasms, Estradiol, Hydrogen-Ion Concentration, Cytochrome P-450 CYP2C8, Isoenzymes, Kinetics, Enzyme Induction, Microsomes, Colonic Neoplasms, Steroid Hydroxylases, Humans, Aryl Hydrocarbon Hydroxylases, Lymphocytes, Cells, Cultured, Cytochrome P-450 CYP2C9, Methylcholanthrene
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