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Timentin and beta-lactamases.

作者信息

Labia R, Morand A, Péduzzi J

出版信息

J Antimicrob Chemother. 1986 May;17 Suppl C:17-26. doi: 10.1093/jac/17.suppl_c.17.

DOI:10.1093/jac/17.suppl_c.17
PMID:3487538
Abstract

Ticarcillin is resistant to the action of cephalosporinases, which explains its biological activity on a large number of bacterial species, including cephalosporinase-producing Enterobacteriaceae and Pseudomonas aeruginosa. Nevertheless, its antibacterial activity is often limited by the action of some beta-lactamases, mostly plasmid-mediated penicillinases. Clavulanic acid by itself has poor antibacterial activity, but its most important property is to inhibit and inactivate beta-lactamases. The inhibitory properties of clavulanic acid were studied on a large number of beta-lactamases. The penicillinases produced by Staphylococcus aureus, the plasmid-mediated beta-lactamases such as the TEM-type, the chromosomally-mediated penicillinases from Klebsiella pneumoniae and other closely-related beta-lactamases, and a few chromosomally-mediated cephalosporinases, such as that produced by Proteus vulgaris, are powerfully inhibited by clavulanic acid. The plasmid-mediated penicillinases of OXA type and most of the chromosomally-mediated cephalosporinases, such as that produced by Escherichia coli (Amp C), are less or poorly inhibited. Moreover, clavulanic acid has some cephalosporinase-inducing properties. These properties are in good agreement with the bacteriological properties of Timentin.

摘要

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