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J Bacteriol. 1969 June; 98(3): 1248-1257
Copyright © 1969 American Society for Microbiology. All Rights Reserved.

Kinetics of Induction and Purification of Chloramphenicol Acetyltransferase from Chloramphenicol-resistant Staphylococcus aureus

E. Winshell and W. V. Shaw1

a Department of Medicine, Columbia University, College of Physicians and Surgeons, New York, New York 10032

ABSTRACT

Plasmid-mediated chloramphenicol resistance in Staphylococcus aureus has been shown to involve acetylation of chloramphenicol by an enzyme induced by growth in the presence of the antibiotic and certain analogues. Analysis of the kinetics of induction has been complicated by (i) the intrinsic inhibitory effects of chloramphenicol on induced enzyme synthesis and (ii) the rapid disappearance of inducer after synthesis of the acetylating enzyme. The compound related to D-threo chloramphenicol which lacks a C3 hydroxyl substituent (3-deoxychloramphenicol) is a potent inducer of chloramphenicol acetyltransferase but is ineffective as an antibiotic and is not a substrate for the enzyme. The availability of such a "gratuitous" inducer has simplified an analysis of the kinetics of induction of chloramphenicol acetyltransferase. The enzyme from induced bacteria has been purified to homogeneity and has been compared with the analogous enzyme present in E. coli which harbors a resistance transfer factor with the chloramphenicol resistance determinant.

FOOTNOTES

1 Present address: Department of Medicine, University of Miami School of Medicine, Miami, Fla. 33152.

J Bacteriol. 1969 June; 98(3): 1248-1257
Copyright © 1969 American Society for Microbiology. All Rights Reserved.





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