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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.
P L Morris, and
T R Burke, and
L R Phol
October 1969,
Life sciences,
P L Morris, and
T R Burke, and
L R Phol
January 1980,
Drug metabolism and disposition: the biological fate of chemicals,
P L Morris, and
T R Burke, and
L R Phol
April 1972,
Nature: New biology,
P L Morris, and
T R Burke, and
L R Phol
January 1980,
Drug metabolism and disposition: the biological fate of chemicals,
P L Morris, and
T R Burke, and
L R Phol
June 1998,
Biochemistry and molecular biology international,
P L Morris, and
T R Burke, and
L R Phol
October 1984,
Chemico-biological interactions,
P L Morris, and
T R Burke, and
L R Phol
February 1978,
Biochemical pharmacology,
P L Morris, and
T R Burke, and
L R Phol
July 1977,
The Journal of biological chemistry,
P L Morris, and
T R Burke, and
L R Phol
August 1981,
Biochemistry,
P L Morris, and
T R Burke, and
L R Phol
May 1985,
British journal of industrial medicine,
