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Characterization of rat and human liver microsomal cytochrome P-450 forms involved in nifedipine oxidation, a prototype for genetic polymorphism in oxidative drug metabolism.
- F. Guengerich, M. Martín, P. Beaune, P. Kremers, T. Wolff, D. Waxman
- Biology, ChemistryThe Journal of biological chemistry
- 15 April 1986
The metabolism of the dihydropyridine calcium antagonist and vasodilator nifedipine has been reported to exhibit polymorphism among individual humans, and the amount of the P-450NF polypeptide may be a major factor in influencing the level of catalytic activity in humans as well as rats.
Purification and characterization of liver microsomal cytochromes p-450: electrophoretic, spectral, catalytic, and immunochemical properties and inducibility of eight isozymes isolated from rats…
- F. Guengerich, G. Dannan, S. Wright, M. Martín, L. Kaminsky
- Biology, ChemistryBiochemistry
- 9 November 1982
The results clearly demonstrate that individual forms of P-450 can be induced by different compounds and that a single compound can lower the level of one form of P -450 while inducing one or more other forms ofP-450.
Roles of individual human cytochrome P-450 enzymes in the bioactivation of benzo(a)pyrene, 7,8-dihydroxy-7,8-dihydrobenzo(a)pyrene, and other dihydrodiol derivatives of polycyclic aromatic…
- T. Shimada, M. Martín, D. Pruess-Schwartz, L. Marnett, F. Guengerich
- Biology, ChemistryCancer research
- 15 November 1989
The roles of the human P-450 enzymes differ from the rodent orthologs in the paradigm for bioactivation of polycyclic hydrocarbons; further, flavones appear to have opposing effects on diol formation and further epoxidation in both human liver and lung.
Cytochrome P-450 enzyme-specific control of the regio- and enantiofacial selectivity of the microsomal arachidonic acid epoxygenase.
Purification and characterization of the human liver cytochromes P-450 involved in debrisoquine 4-hydroxylation and phenacetin O-deethylation, two prototypes for genetic polymorphism in oxidative…
Random mutagenesis of human cytochrome p450 2A6 and screening with indole oxidation products.
- K. Nakamura, M. Martín, F. Guengerich
- Biology, ChemistryArchives of biochemistry and biophysics
- 1 November 2001
Cytochrome P450 (P450) 2A6 mutants from randomized libraries generated in the substrate recognition sequence (SRS) regions were screened in Escherichia coli on the basis of indole metabolism and yielded mixtures of pigments from indole different than WT, as judged by visible spectra and HPLC of products.
Expression of modified human cytochrome P450 1A2 in Escherichia coli: stabilization, purification, spectral characterization, and catalytic activities of the enzyme.
- P. Sandhu, Z. Guo, T. Baba, M. Martín, R. Tukey, F. Guengerich
- BiologyArchives of biochemistry and biophysics
- 1 February 1994
The expressed human P450 1A2 in bacterial membranes was rapidly denatured to cytochrome P420 in the presence of detergents, and the enzyme was catalytically active toward the known substrates 7-ethoxyresorufin and phenacetin.
Activation of heterocyclic aromatic amines by rat and human liver microsomes and by purified rat and human cytochrome P450 1A2.
- R. Turesky, A. Constable, F. Guengerich
- Biology, ChemistryChemical research in toxicology
- 30 July 1998
Cytochrome P450 1A2 expression in rodent and human liver tissue varies greatly and there are considerable differences between the enzymes in the two species in the activation of some heterocyclic aromatic amines, which must be considered when assessing human health risk.
Cytochrome P-450-dependent oxidation of arachidonic acid to 16-, 17-, and 18-hydroxyeicosatetraenoic acids.