Characterization of Chloramphenicol Acetyltransferase from Chloramphenicol-resistant Staphylococcus aureus

Publisher Website
Google Scholar
Abstract
Chloramphenicol-resistant strains of S. aureus contain an inducible enzyme which inactivates chloramphenicol by acetylation in the presence of acetyl CoA. 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 acetyl transferase are complicated by the inducer''s effect on biosynthesis and its fate as chloramphenicol 3-acetate, which is not an in-ducer of the enzyme. The E. coli and S. aureus enzymes were 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. Anti-serum 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.

This publication has 19 references indexed in Scilit: