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Antimicrob Agents Chemother. 1973 February; 3(2): 289-298
Copyright © 1973 American Society for Microbiology. All Rights Reserved.
a Service de Microbiologie, Faculté de Médecine, Institut de Botanique, Université de Liège, Sart-Tilman, 4000 Liège, Belgium
ABSTRACT
The ß-lactamases excreted by the highly benzylpenicillin-susceptible Streptomyces strain R39 and the highly benzylpenicillin-resistant Streptomyces albus G were isolated and purified. Neither ß-lactamase exhibited DD-carboxypeptidase activity. Both were anionic at pH 8.3, did not require metal ions, and were not sensitive to iodine, but were inhibited by Cu2+ and readily inactivated by heat. p-Chloromercuribenzoate, iodoacetate, p-aminobenzoate, and substrates and inhibitors of DD-carboxypeptidase had no effect on ß-lactamase activity. The Km and Vmax values for ß-lactamase activity were studied with 6-aminopenicillanic acid and with various penicillins and cephalosporins. The ß-lactamase from the related strain K11 of Streptomyces, which is intermediate in its susceptibility to benzylpenicillin, was partially purified, and its activity was compared on the various substrates.
1 Permanent address: Division of Biological Sciences, National Research Council of Canada, Ottawa Ontario, Canada.
2 Permanent address: Department of Microbiology, University of Alberta, Edmonton, Alberta, Canada.
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