Title : Cytochrome P-450 2B6 is responsible for interindividual variability of propofol hydroxylation by human liver microsomes.

Pub. Date : 2001 Jan

PMID : 11135730






5 Functional Relationships(s)
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1 Cytochrome P-450 2B6 is responsible for interindividual variability of propofol hydroxylation by human liver microsomes. Propofol cytochrome P450 family 2 subfamily B member 6 Homo sapiens
2 RESULTS: Propofol hydroxylation by hepatic microsomes showed more than 19-fold variability and was most closely correlated to CYP2B6 protein content (r = 0.904), and the CYP2B6 marker activities, S-mephenytoin N-demethylation (r = 0.919) and bupropion hydroxylation (r = 0.854). Propofol cytochrome P450 family 2 subfamily B member 6 Homo sapiens
3 RESULTS: Propofol hydroxylation by hepatic microsomes showed more than 19-fold variability and was most closely correlated to CYP2B6 protein content (r = 0.904), and the CYP2B6 marker activities, S-mephenytoin N-demethylation (r = 0.919) and bupropion hydroxylation (r = 0.854). Propofol cytochrome P450 family 2 subfamily B member 6 Homo sapiens
4 All of the CYPs evaluated were capable of hydroxylating propofol; however, CYP2B6 and CYP2C9 were most active. Propofol cytochrome P450 family 2 subfamily B member 6 Homo sapiens
5 CONCLUSIONS: Cytochrome P-450 2B6, and to a lesser extent CYP2C9, contribute to the oxidative metabolism of propofol. Propofol cytochrome P450 family 2 subfamily B member 6 Homo sapiens