Glutathione-dependent dechlorination of chloramphenicol by cytosol of rat liver

J. L. Martin, J. W. George, L. R. Pohl

Research output: Contribution to journalArticle

Abstract

The 100,000 g supernatant fraction (cytosol) of rat liver converts chloramphenicol (CAP, RNHCOCHCl2) into two products. Most of the enzyme activity is lost during dialysis of the enzyme preparation overnight, but is restored by addition of glutathione (GSH). Other thiols are not as effective as GSH in restoring the enzyme activity. The formation of the metabolites is not inhibited when incubations are performed under anaerobic conditions. The major metabolite was identified as CAP aldehyde (RNHCOCHO) whereas the minor metabolite was identified as an alkali-unstable derivative of CAP oxamic acid (RNHCOCOOH). Plausible pathways are discussed for the formation of these metabolites.

Original languageEnglish (US)
Pages (from-to)93-97
Number of pages5
JournalDrug Metabolism and Disposition
Volume8
Issue number2
StatePublished - 1980
Externally publishedYes

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Dechlorination
Chloramphenicol
Metabolites
Liver
Cytosol
Glutathione
Rats
Oxamic Acid
Enzyme activity
Enzymes
Alkalies
Sulfhydryl Compounds
Aldehydes
Dialysis
Derivatives

ASJC Scopus subject areas

  • Pharmacology
  • Toxicology

Cite this

Glutathione-dependent dechlorination of chloramphenicol by cytosol of rat liver. / Martin, J. L.; George, J. W.; Pohl, L. R.

In: Drug Metabolism and Disposition, Vol. 8, No. 2, 1980, p. 93-97.

Research output: Contribution to journalArticle

Martin, J. L. ; George, J. W. ; Pohl, L. R. / Glutathione-dependent dechlorination of chloramphenicol by cytosol of rat liver. In: Drug Metabolism and Disposition. 1980 ; Vol. 8, No. 2. pp. 93-97.
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