Influence of Spontaneous and Inducible β-Lactamase Production on the Antimicrobial Activity of Recently Developed β-Lactam Compounds
- 1 January 1984
- journal article
- research article
- Published by S. Karger AG in Chemotherapy
- Vol. 30 (3), 175-181
- https://doi.org/10.1159/000238265
Abstract
The activity of 9 recently developed β-lactam compounds was evaluated in 185 ampicillin-resistant isolates of Enterobacteriaceae. Moreover, in all strains, spontaneous and inducible β-lactamase production was quantified and correlated with the minimal inhibitory concentration (MIC) of each compound. In most species, no correlation could be observed between spontaneoulsy produced β-lactamase and the MICs, with the only exceptions of Serratia spp. and Morganella morganii isolates for methoxyimino cephalosporins and azthreonam. On the other hand, the increase of MICs of third-generation cephalosporins and azthreonam correlated well with the total amount of enzyme produced. With respect to temocillin and the penem compound Sch 29 482, there was a significant correlation of enzyme production and MICs only among the Citrobacter spp. isolates. It can be assumed that the effectiveness of the new agents is not only due to the low rate of hydrolysis, but also to the rapid binding to the lethal target.Keywords
This publication has 5 references indexed in Scilit:
- Growth curve patterns and bacterial morphology of Escherichia coli subjected to different temocillin (BRL17421) concentrationsJournal of Antimicrobial Chemotherapy, 1982
- A comparison of the antibacterial activities of N-formimidoyl thienamycin (MK0787) with those of other recently developed beta-lactam derivativesAntimicrobial Agents and Chemotherapy, 1982
- Penem derivatives: beta-lactamase stability and affinity for penicillin-binding proteins in Escherichia coliAntimicrobial Agents and Chemotherapy, 1982
- Sch 29482: Stability and inhibitory potency towards -lactamases from Gram-negative bacteriaJournal of Antimicrobial Chemotherapy, 1982
- A modification of the Lowry procedure to simplify protein determination in membrane and lipoprotein samplesAnalytical Biochemistry, 1978