In vitro metabolism of chloroquine: identification of CYP2C8, CYP3A4, and CYP2D6 as the main isoforms catalyzing N-desethylchloroquine formation. [electronic resource]
Producer: 20040112Description: 748-54 p. digitalISSN:- 0090-9556
- Animals
- Aryl Hydrocarbon Hydroxylases -- antagonists & inhibitors
- Biotransformation
- Cells, Cultured
- Chloroquine -- analogs & derivatives
- Chromatography, High Pressure Liquid
- Cytochrome P-450 CYP2C8
- Cytochrome P-450 CYP2D6 -- biosynthesis
- Cytochrome P-450 CYP2D6 Inhibitors
- Cytochrome P-450 CYP3A
- Cytochrome P-450 Enzyme Inhibitors
- Cytochrome P-450 Enzyme System -- biosynthesis
- Enzyme Inhibitors -- pharmacology
- Humans
- Insecta
- Isoenzymes -- antagonists & inhibitors
- Kinetics
- Microsomes, Liver -- drug effects
- Recombinant Proteins -- antagonists & inhibitors
- Spectrometry, Mass, Electrospray Ionization
- Transfection
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Publication Type: Journal Article; Research Support, Non-U.S. Gov't
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