Reductive dechlorination of chloramphenicol by rat liver microsomes.
When chloramphenicol was incubated with rat liver microsomes anaerobically, it was metabolized predominantly to deschloro-chloramphenicol and products that become irreversibly bound to microsomal protein. Cytochromes P-450 induced by phenobarbital appeared to catalyze these reactions most effectively. Glutathione increased the formation of deschloro-chloramphenicol by 13% and decreased the amount of the irreversibly bound product by 18%, respectively. Only a small amount of the nitroaromatic-reduced product, chloramphenicol amine, was detected by high pressure liquid chromatography. These results are consistent with chloramphenicol being biotransformed and activated by cytochromes P-450 anaerobically through predominantly reductive dechlorination.
D000332:Aerobiosis; D000693:Anaerobiosis; D000818:Animals; D001711:Biotransformation; D002701:Chloramphenicol / Q000378:metabolism*; D002713:Chlorine / Q000378:metabolism; D002851:Chromatography, High Pressure Liquid; D066298:In Vitro Techniques; D008297:Male; D013058:Mass Spectrometry; D008862:Microsomes, Liver / Q000378:metabolism*; D010084:Oxidation-Reduction; D051381:Rats; D011919:Rats, Inbred Strains
D002713:Chlorine; D002701:Chloramphenicol