Specificity of substrate and inhibitor probes for human cytochromes P450 1A1 and 1A2.
- W. Tassaneeyakul, D. Birkett, J. Miners
- Biology, ChemistryJournal of Pharmacology and Experimental…
- 1 April 1993
The results indicate that the majority of human CYP 1A xenobiotic inhibitor and substrate probes are nonspecific in their recognition of CYP1A1 and CYp1A2, although selectivity is apparent for some compounds.
Tolbutamide hydroxylation by human liver microsomes. Kinetic characterisation and relationship to other cytochrome P-450 dependent xenobiotic oxidations.
- J. Miners, K. Smith, R. Robson, M. McManus, M. E. Veronese, D. Birkett
- Biology, ChemistryBiochemical Pharmacology
- 15 March 1988
Diazepam metabolism by human liver microsomes is mediated by both S-mephenytoin hydroxylase and CYP3A isoforms.
- T. Andersson, J. Miners, M. E. Veronese, D. Birkett
- Chemistry, BiologyBritish Journal of Clinical Pharmacology
- 1 August 1994
Studies with a series of CYP isoform selective inhibitors and with an inhibitory anti-CYP2C antibody indicated that temazepam formation was carried out mainly by CYP3A isoforms, whereas the formation of N-desmethyldiazepam was mediated by both CYP2C isoforms and S-mephenytoin hydroxylase.
Allelic variants of human cytochrome P450 2C9: baculovirus-mediated expression, purification, structural characterization, substrate stereoselectivity, and prochiral selectivity of the wild-type and…
- R. Haining, A. P. Hunter, M. E. Veronese, W. Trager, A. Rettie
- BiologyArchives of Biochemistry and Biophysics
- 15 September 1996
The greatly decreased catalytic efficiency of the I359L variant suggests that leucine homozygotes would eliminate (S)-warfarin, and probably many other CYP2C9 substrates, at much slower rates in vivo than individuals expressing the wild-type enzyme.
Validation of the tolbutamide metabolic ratio for population screening with use of sulfaphenazole to produce model phenotypic poor metabolizers
- M. E. Veronese, J. Miners, D. Randles, D. Gregov, D. Birkett
- Medicine, BiologyClinical pharmacology and therapy
- 1 March 1990
The tolbutamide urinary metabolic ratio effectively distinguishes tol butamide hydroxylase activity in “normal” subjects and in those converted to model phenotypically “poor” metabolizers by sulfaphenazole.
Identification of human liver cytochrome P450 isoforms mediating omeprazole metabolism.
- T. Andersson, J. Miners, M. E. Veronese, W. Tassaneeyakul, U. Meyer, D. Birkett
- Biology, ChemistryBritish Journal of Clinical Pharmacology
- 1 December 1993
The results predict that omeprazole clearance in vivo would be reduced in poor metabolisers of mephenytoin due to reduction in the dominant partial metabolic clearance to hydroxyomeprazole.
Validation of 4-nitrophenol as an in vitro substrate probe for human liver CYP2E1 using cDNA expression and microsomal kinetic techniques.
- W. Tassaneeyakul, M. E. Veronese, D. Birkett, F. Gonzalez, J. Miners
- Biology, ChemistryBiochemical Pharmacology
- 3 December 1993
Identification of human liver cytochrome P450 isoforms mediating secondary omeprazole metabolism.
- T. Andersson, J. Miners, M. E. Veronese, D. Birkett
- Biology, ChemistryBritish Journal of Clinical Pharmacology
- 1 June 1994
Inhibition studies, with a series of isoform selective inhibitors as well as with an anti-CYP2C3 antibody, suggested a dominant role of S-mephenytoin hydroxylase in the formation of hydroxysulphone from omeprazole sulphone.
Caffeine metabolism by human hepatic cytochromes P450: contributions of 1A2, 2E1 and 3A isoforms.
- W. Tassaneeyakul, D. Birkett, J. Miners
- Chemistry, BiologyBiochemical Pharmacology
- 18 May 1994
Site-directed mutation studies of human liver cytochrome P-450 isoenzymes in the CYP2C subfamily.
- M. E. Veronese, C. Doecke, D. Birkett
- Biology, ChemistryBiochemical Journal
- 15 January 1993
It is concluded that, although 2C8 and 2C9/10 proteins metabolize tolbutamide, only 1C9 or 1C10 proteins play a major role in human liver, and subtle differences in the amino acid composition of these 2C 9/ 10 proteins can affect the functional specificities towards both tol butamide and phenytoin.
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