Chloramphenicol: an enzymological microassay

P. S. Lietman, T. J. White, W. V. Shaw

Research output: Contribution to journalArticle

Abstract

A new assay for chloramphenicol in biological fluids has been developed that offers sensitivity, specificity, precision, accuracy, economy, and ease of performance. The assay is based on the enzymological acetylation of chloramphenicol catalyzed by an R factor mediated enzyme. [14C]acetyl coenzyme A serves as the donor of the labeled acetyl group, and the product, [14C]acetoxychloramphenicol, is separated from the labeled precursor by utilizing its preferential extraction into benzene. The product is then quantified by liquid scintillation counting. This assay measures chloramphenicol concentrations in both plasma and other biological specimens and in the presence of other antibiotics, hemolysis, or jaundice. Its rapidity and ease of performance are useful for clinical laboratories, and its sensitivity allows determinations on 10 μl of plasma.

Original languageEnglish (US)
Pages (from-to)347-353
Number of pages7
JournalAntimicrobial agents and chemotherapy
Volume10
Issue number2
DOIs
StatePublished - 1976

ASJC Scopus subject areas

  • Pharmacology
  • Pharmacology (medical)
  • Infectious Diseases

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