Metabolism of dichloromethane and the subsequent binding of its product, carbon monoxide, to cytochrome P-450 in perfused rat liver.
The interaction of cytochrome P-450 and dichloromethane (DCM) was investigated spectrophotometrically in the perfused rat liver. DCM bound to cytochrome P-450 and showed a type I spectral change, with a peak at 450 nm. The peak at 450 nm was developed by addition of exogenous carbon monoxide (CO) to the perfusate. By examining the pattern of the spectral change, we concluded that CO formed during DCM metabolism by cytochrome P-450 bound to cytochrome P-450 in the perfused liver.
Takano
T
T
Department of Public Health and Environmental Science, Faculty of Medicine, Tokyo Medical and Dental University, Japan.
Miyazaki
Y
Y
D000818:Animals; D002248:Carbon Monoxide / Q000378:metabolism*; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism*; D006843:Hydrocarbons, Chlorinated / Q000378:metabolism*; D008099:Liver / Q000378:metabolism*; D008297:Male; D008752:Methylene Chloride / Q000378:metabolism*; D010477:Perfusion; D051381:Rats; D013057:Spectrum Analysis; D013997:Time Factors
D006843:Hydrocarbons, Chlorinated; D008752:Methylene Chloride; D002248:Carbon Monoxide; D003577:Cytochrome P-450 Enzyme System