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Molecular Specificities of R Factor-Determined Beta-Lactamases: Correlation with Plasmid Compatibility

¹ Department of Bacteriology, Royal Postgraduate Medical School, Ducane Road, London W12 OHS England; Department of Bacteriology, Clinic of Therapeutics, University of Athens, Athens, Greece; and Microbiology Section, Department of Pharmaceutics, The School of Pharmacy University of London, London WC1N 1AX, England

ABSTRACT

Beta (ß)-lactamases determined by 29 ampicillin resistance plasmids could be divided into two types. One, TEM-type, was very uniform with respect to substrate specificity but heterogeneous in absolute levels of ß-lactamase activity. The TEM-type ß-lactamase was determined by R factors of compatibility groups FII, I, I, N, C, A, T, W, P, L, and X, and by prophage Amp. The other type, characterized by the ability to hydrolyze oxacillin, was less common, showed lower absolute levels of activity, and was heterogeneous as regards substrate specificities. Oxacillin-hydrolyzing ß-lactamases were determined by R factors of compatibility groups FI, I, N, C, and O.

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