| Literature DB >> 2109582 |
I Szabó1, J Barabás, A Tar, L Kiss, M Filep, T Schmidt, K Marossy, B Tóth-Martinez, G Barabás, F Hernádi.
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.Entities:
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Year: 1990 PMID: 2109582 PMCID: PMC171585 DOI: 10.1128/AAC.34.2.349
Source DB: PubMed Journal: Antimicrob Agents Chemother ISSN: 0066-4804 Impact factor: 5.191