JB
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Shaw, W. V.
Right arrow Articles by Sands, L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Shaw, W. V.
Right arrow Articles by Sands, L.

 Previous Article  |  Next Article 

J Bacteriol. 1970 December; 104(3): 1095-1105
Copyright © 1970 American Society for Microbiology. All Rights Reserved.

Mechanism of Chloramphenicol Resistance in Staphylococcus epidermidis

W. V. Shaw1, D. W. Bentley2 and L. Sands3

1 Department of Medicine, University of Miami School of Medicine, Miami, Florida 33152
2 Department of Biochemistry, University of Miami School of Medicine, Miami, Florida 33152
Veterans Administration (Westside) Hospital, and University of Illinois College of Medicine, Chicago, Illinois 60680

ABSTRACT

The mechanism of chloramphenicol resistance in several multiple-resistant Staphylococcus epidermidis strains has been studied and shown to be due to the presence of the enzyme, chloramphenicol acetyltransferase. As with S. aureus, the inactivating enzyme in S. epidermidis appears to be the product of a structural gene on the chloramphenicol plasmid because resistance and enzyme activity are concurcurrently lost after growth in acridine orange or at elevated temperatures. The synthesis of chloramphenicol acetyltransferase in S. epidermidis has been compared with the function of a similar enzyme in chloramphenicol-resistant S. aureus with the conclusion that the kinetics of induction, products of the reaction, and general properties of the enzymes are identical. The chloramphenicol acetylating enzyme from S. epidermidis has been purified to a state of homogeneity and compared with the analogous purified S. aureus enzyme. Both purified preparations consist of native enzymes with molecular weights of 80,000, and evidence is presented that is consistent with their being made up of four identical subunits of 20,000 each. The two staphylococcal enzymes are identical with respect to pH optimum, apparent affinity (Km) for chloramphenicol, heat denaturation, and immunological reactivity, but they differ in electrophoretic mobility, chromatographic behavior, substrate specificity, and sensitivity to inhibition by mercuric ion.

J Bacteriol. 1970 December; 104(3): 1095-1105
Copyright © 1970 American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:



Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
Appl. Environ. Microbiol. Infect. Immun. Eukaryot. Cell
Mol. Cell. Biol. J. Virol. Microbiol. Mol. Biol. Rev.
ALL ASM JOURNALS

Copyright © 1970 by the American Society for Microbiology. All rights reserved.