Affiliation:
1. Institute of Biology, University Medical School, Debrecen, Hungary.
Abstract
The antibacterial activity of BK-218 was similar to that of cefamandole when it was tested against several laboratory strains. The inhibiting effect of BK-218 was greater than that of cephalexin and cefoxitin on penicillin-binding proteins of Escherichia coli HB101. This result was in close correlation with the relative inhibition of radiolabeled glucosamine incorporation (greatest with BK-218) and with the lytic effect (most intensive with BK-218). BK-218 proved to be a good inhibitor for all five of the beta-lactamases that were investigated, although two enzymes (Enterobacter cloacae P99 and Pseudomonas aeruginosa Cilote) hydrolyzed it to some extent.
Publisher
American Society for Microbiology
Subject
Infectious Diseases,Pharmacology (medical),Pharmacology
Reference34 articles.
1. Experiments on the degradation of cephalosporin C;Abraham E. P.;Biochem. J.,1956
2. Abraham E. P. and S. G. Waley. 1979. Beta-lactamases from Bacillus cereus p. 311-338. In J. M. T. Hamilton-Miller and J. T. Smith (ed.) Beta-lactamases. Academic Press Inc. (London) Ltd. London.
3. Isolation and properties of an inducible and a constitutive beta-lactamase from Pseudomonas aeruginosa;Berks M.;J. Gen. Microbiol.,1982
4. Comparison of in vitro activity of cephalexin, cephadrine, and cefaclor;Bill N. J.;Antimicrob. Agents Chemother.,1977
5. A film detection method for tritium labelled proteins and nucleic acids in polyacrylamide gels;Bonner W. M.;Eur. J. Biochem.,1974
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