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Role of human cytochrome P-450 IIE1 in the oxidation of many low molecular weight cancer suspects.
TLDR
The results collectively indicate that P-450 IIE1 is a major catalyst of the oxidation of benzene, styrene, CCl4, CHCl3, CH2Cl2, CH3Cl, 1,2-dichloropropane, ethylene dichloride, vinyl chloride, vinyl bromide, acrylonitrile, vinyl carbamate, ethylcarbamate, and trichloroethylene.
Studies on the expression and metabolic capabilities of human liver cytochrome P450IIIA5 (HLp3).
TLDR
It was observed that P450IIIA5 was detected in a statistically significantly higher percentage of children and adolescents (19 years old and under), as compared with the remaining population (8 of 17, 47%, versus 11 of 46, 24%, respectively).
Hydroxylation of chlorzoxazone as a specific probe for human liver cytochrome P-450IIE1.
TLDR
Results provide strong evidence that P-450IIE1 is the primary catalyst of chlorzoxazone 6-hydroxylation in human liver and may have potential use as a noninvasive probe in estimating the in vivo expression of the protein.
Human cytochrome P-450PA (P-450IA2), the phenacetin O-deethylase, is primarily responsible for the hepatic 3-demethylation of caffeine and N-oxidation of carcinogenic arylamines.
TLDR
Estimation of caffeine 3-demethylation activity in humans may be useful in the characterization of arylamine N-oxidation phenotypes and in the assessment of whether or not the hepatic levels of cytochrome P-450PA, as affected by environmental or genetic factors, contribute to interindividual differences in susceptibility to arieslamine-induced cancers.
Hydroxylation of chlorzoxazone as a specific probe for human liver cytochrome P-450IIE1
TLDR
Results provide strong evidence that P-450IIE1 is the primary catalyst of chlorzoxazone 6-hydroxylation in human liver and may have potential use as a noninvasive probe in estimating the in vivo expression of the protein.
Oxidation of dihydropyridine calcium channel blockers and analogues by human liver cytochrome P-450 IIIA4.
TLDR
The results indicate that the enzyme P-450 IIIA4 is probably the major human catalyst involved in the formal dehydrogenation of most but not all 1,4-dihydropyridine drugs.
Catalytic activities of human liver cytochrome P-450 IIIA4 expressed in Saccharomyces cerevisiae.
TLDR
The results of these studies with a defined protein clearly demonstrate the ability of P-450 IIIA4 to catalyze regio- and stereoselective oxidations with a diverse group of substrates, and this enzyme appears to be one of the most versatile catalysts in the P- 450 family.
Human liver microsomal cytochrome P-450 enzymes involved in the bioactivation of procarcinogens detected by umu gene response in Salmonella typhimurium TA 1535/pSK1002.
TLDR
The literature suggests that the two human liver P-450s involved in activation of these 16 procarcinogens are highly inducible by barbiturates, macrolide antibodies, and certain steroids and by smoking and ingestion of charcoal-containing food (P-450PA).
Cynomolgus monkey cytochrome P450 2C43: cDNA cloning, heterologous expression, purification and characterization.
TLDR
The cDNA of cytochrome P450 (CYP) 2C43 was cloned from cynomolgus monkey liver by RT-PCR and deduced amino acid sequence showed 93% and 91% identity to human CYP2C9 and CYP 2C19, respectively, indicating that CYP1C43 is similar to CYP3C19 rather than CYP8C9.
Site-directed mutagenesis of mouse steroid 7 alpha-hydroxylase (cytochrome P-450(7) alpha): role of residue-209 in determining steroid-cytochrome P-450 interaction.
TLDR
The results indicate, therefore, that the identity of residue 209 determines the affinity as well as specificity of steroid binding to both P450(7) alpha and P 450(15) alpha.
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