Author: Marini S. Grasso E. Longo V. Puccini P. Riccardi B. Giovanni Gervasi P.
Publisher: Informa Healthcare
ISSN: 1366-5928
Source: Xenobiotica, Vol.33, Iss.1, 2003-01, pp. : 1-11
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Abstract
1. 4-Biphenylaldehyde (4-BA) and 9-anthraldehyde (9-AA) were examined as substrates for cytochrome P450 (CYPs) enzymes in rat and human. Both aldehydes were oxidized by CYPs to fluorescent carboxylic acids, which can be assayed with a high sensitivity by an easy fluorimetric method.2. With liver microsomes from control and induced rats, the oxidation of both 9-AA and 4-BA followed simple Michaelis-Menten kinetics. Only microsomes from rats pretreated with phenobarbital (a strong inducer of P4502B1/2) could increase (about threefold) the oxidation rates (Vmax) of both aldehydes above the control values, which were 6.7±1.1 and 3.3±0.6 nmol min−1 mg−1 protein for 4-BA and 9-AA, respectively. On the other hand, the Km's, which were similar for both aldehydes (about 25 µM), did not change significantly with any inducer. The use of purified rat CYP1A1, 2E1, 2B1 and 2C11 in a reconstituted system showed that only 2B1 and 2C11 could oxidize both substrates with a high turnover.3. In human liver microsomes, the oxidation rates of these aldehydes (1.6±0.2 and 0.42±0.1 nmol min−1 mg−1 protein for 4-BA and 9-AA, respectively) were lower than those of rat but with similar K
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