Timentin and -lactamases
- 1 January 1986
- journal article
- research article
- Published by Oxford University Press (OUP) in Journal of Antimicrobial Chemotherapy
- Vol. 17 (suppl C) , 17-26
- https://doi.org/10.1093/jac/17.suppl_c.17
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 β -lactamases, mostly plasmid-mediated penicillinases. Clavulanic acid by itself has poor antibacterial activity, but its most important property is to inhibit and inactivate β -lactamases. The inhibitory properties of clavulanic acid were studied on a large number of β -lactamases. The penicillinases produced by Staphylococcus aureus , the plasmid-mediated β -lactamases such as the TEM-type, the chromosomally-mediated penicillinases from Klebsiella pneumoniae and other closely-related β -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.Keywords
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