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Antimicrob Agents Chemother. 1973 February; 3(2): 299-305
Copyright © 1973 American Society for Microbiology. All Rights Reserved.

Mechanism of Chloramphenicol Resistance in Staphylococci: Characterization and Hybridization of Variants of Chloramphenicol Acetyltransferase

L. C. Sands and W. V. Shaw

Department of Medicine, University of Miami School of Medicine, Miami, Florida 33152
Department of Biochemistry, University of Miami School of Medicine, Miami, Florida 33152

ABSTRACT

Fifty clinical isolates of chloramphenicol-resistant staphylococci from diverse sources were screened for the presence of chloramphenicol acetyltransferase (CAT) and were found to contain the inducible chloramphenicol-inactivating enzyme in each case. Polyacrylamide disc gel electrophoresis revealed four distinct types of CAT of which three were purified to a state of homogeneity. Each purified CAT preparation was shown to exist as a tetrameric protein with a native molecular weight of 80,000 and an identical subunit size of 20,000. All four staphylococcal types of CAT exhibited identical catalytic and immunological properties, but they possessed variable sensitivity to heat denaturation and to inhibition by mercuric ion. Each of the three purified variants of staphylococcal CAT was capable of undergoing reversible denaturation in 6 M guanidine hydrochloride. In vitro hybridization was successful between pairs of each of the three purified staphylococcal enzymes. Only one heteromeric (hybrid) species was observed in addition to the parental types rather than the three predicted from the known quaternary structure of staphylococcal CAT.

Antimicrob Agents Chemother. 1973 February; 3(2): 299-305
Copyright © 1973 American Society for Microbiology. All Rights Reserved.





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