Major cytochrome P450 enzyme responsible for oxidation of secondary alcohols to the corresponding ketones in mouse hepatic microsomes: Oxidation of 7-hydroxy-Δ8-tetrahydrocannabinol to 7-oxo-Δ8-tetrahydrocannabinol

Tamihide Matsunaga, Nobuyuki Kishi, Hiroyuki Tanaka, Kazuhito Watanabe, Hidetoshi Yoshimura, Ikuo Yamamoto

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Abstract

The oxidative activities of 7α- and 7β-hydroxy-Δ8- tetrahydrocannabinol (7α- and 7β-hydroxy-Δ8-THC) to 7-oxo-Δ8-THC in hepatic microsomes of mice were significantly increased by the treatment of mice with dexamethasone or phenobarbital. A cytochrome P450 enzyme, named P450MDX-B, was purified from hepatic microsomes of dexamethasone-treated mice, and its apparent molecular mass was estimated to be 51,000. The NH2- terminal amino acid sequence of P450MDX-B was the same as that of CYP3A11. The oxidative activities of 7α- and 7β-hydroxy-Δ8-THC were 2.55 and 4.92 nmol/min/nmol P450, respectively. The antibody against P450MDX-B almost completely inhibited the oxidative activities of 7α- and 7β-hydroxy-Δ8- THC in mice. These results indicate that P450MDX-B (CYP3A11) is a major enzyme responsible for the oxidation of 7α- and 7β-hydroxy-Δ8-THC to 7- oxo-Δ8-THC in mouse liver.

Original languageEnglish
Pages (from-to)1045-1047
Number of pages3
JournalDrug Metabolism and Disposition
Volume26
Issue number10
Publication statusPublished - Oct 1 1998

All Science Journal Classification (ASJC) codes

  • Pharmacology
  • Pharmaceutical Science

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