1. Metabolism of Chamaechromone In Vitro with Human Liver Microsomes and Recombinant Human Drug-Metabolizing Enzymes
- Author
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Haihong Hu, Jinqi Zheng, Yan Lou, Su Zeng, Linrun Wang, Xingguo Zhang, and Yunqing Qiu
- Subjects
Metabolite ,Glucuronidation ,Pharmaceutical Science ,Naphthols ,In Vitro Techniques ,Pharmacology ,Biology ,Hydroxylation ,Antiviral Agents ,Plant Roots ,Analytical Chemistry ,law.invention ,chemistry.chemical_compound ,Cytochrome P-450 CYP1A2 ,law ,Drug Discovery ,Humans ,Drug Interactions ,Enzyme kinetics ,Glucuronosyltransferase ,Fluconazole ,Benzoflavones ,Organic Chemistry ,Metabolism ,Flavones ,Recombinant Proteins ,Liver ,Complementary and alternative medicine ,Biochemistry ,chemistry ,Thymelaeaceae ,Microsomes, Liver ,Microsome ,Recombinant DNA ,Molecular Medicine ,Quercetin ,Drugs, Chinese Herbal - Abstract
Chamaechromone is a major component in the dried roots of Stellera chamaejasme with antihepatitis B virus and insecticidal activity. In this study, metabolic profiles of chamaechromone were investigated in human liver microsomes. One monohydroxide and two monoglucuronides of chamaechromone were identified. The enzyme kinetics for both hydroxylation and glucuronidation were fitted to the Michaelis–Menten equation. The hydroxylation of chamaechromone was inhibited by α -naphthoflavone, and predominantly catalyzed by recombinant human cytochrome P450 1A2, whereas the glucuronidation was inhibited by quercetin, 1-naphthol, and fluconazole, and mainly catalyzed by recombinant human UDP-glucuronosyltransferase 1A3, 1A7, 1A9, and 2B7.
- Published
- 2014