Anaerobic dehalogenation of halothane by reconstituted liver microsomal cytochrome P-450 enzyme system |
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Authors: | K Fujii N Miki T Sugiyama M Morio T Yamano Y Miyake |
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Affiliation: | 1. Department of Biochemistry, National Cardiovascular Center Research Institute, Fujishiro-dai, Suita, 565, Japan;2. Department of Anesthesiology, Medical School of Hiroshima University, Minami-ku, Hiroshima, 734, Japan;3. Department of Biochemistry, Medical School of Osaka University, Kita-ku, Osaka, 530, Japan |
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Abstract: | Cytochrome P-450 from liver microsomes of phenobarbital-treated rabbits catalyzed anaerobic dehalogenation of halothane (2-bromo-2-chloro-1,1,1-trifluoroethane) when combined with NADPH and NADPH-cytochrome P-450 reductase. Cytochromes P-450B1 and P-448 from liver microsomes of untreated rabbits were less active. Triton X-100 accelerated the reaction. Unlike anaerobic dehalogenation of halothane in microsomes, the major product was 2-chloro-1,1,1-trifluoroethane and 2-chloro-1,1-difluoroethylene was negligible. These products were not detected under aerobic conditions, and dehalogenation activity was inhibited by carbon monoxide, phenyl isocyanide and metyrapone. |
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Keywords: | To whom all correspondence should be addressed. |
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