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. 1968 Jan;95(1):28–36. doi: 10.1128/jb.95.1.28-36.1968

Characterization of Chloramphenicol Acetyltransferase from Chloramphenicol-resistant Staphylococcus aureus

W V Shaw 1, R F Brodsky 1
PMCID: PMC251967  PMID: 4965980

Abstract

Chloramphenicol-resistant strains of Staphylococcus aureus contain an inducible enzyme which inactivates chloramphenicol by acetylation in the presence of acetyl coenzyme A. The products of acetylation are chromatographically indistinguishable from those obtained with chloramphenicol-resistant Escherichia coli harboring an R factor. The kinetics of induction of chloramphenicol acetyltransferase are complicated by the inducer's effect on protein biosynthesis and its fate as chloramphenicol 3-acetate, which is not an inducer of the enzyme. The E. coli and S. aureus enzymes have been compared, with the conclusion that they are identical with respect to molecular weight (approximately 78,000) and pH optimum (7.8), but differ with respect to heat stability, substrate affinity, electrophoretic mobility, and immunological reactivity. Antiserum prepared against enzyme from E. coli contains precipitating antibody, which inactivates the E. coli enzyme, but neither precipitates nor neutralizes the activity of S. aureus enzyme.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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