Title : Differential activities of CYP1A isozymes in hepatic and intestinal microsomes of control and 3-methylcholanthrene-induced rats.

Pub. Date : 2000 Feb

PMID : 10728918






3 Functional Relationships(s)
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1 Caffeine metabolism and inhibition studies by furafylline, CYP1A1 antiserum and ketoconazole revealed that the differences in the expression of CYP1A1 and CYP1A2 in the two tissues led to significant changes in the contribution of the various isoenzymes involved in the biotransformation of caffeine. Caffeine cytochrome P450, family 1, subfamily a, polypeptide 2 Rattus norvegicus
2 Caffeine metabolism and inhibition studies by furafylline, CYP1A1 antiserum and ketoconazole revealed that the differences in the expression of CYP1A1 and CYP1A2 in the two tissues led to significant changes in the contribution of the various isoenzymes involved in the biotransformation of caffeine. Caffeine cytochrome P450, family 1, subfamily a, polypeptide 2 Rattus norvegicus
3 Furthermore in rat intestine cytochrome P450 isozymes such as CYP1A1 and CYP3A replace CYP1A2 in the caffeine metabolism. Caffeine cytochrome P450, family 1, subfamily a, polypeptide 2 Rattus norvegicus