Abstract
Evaluation of four β-lactamase inhibitors in terms of their outer membrane permeability in Pseudomonas aeruginosa revealed that sulbactam and tazobactam diffused most efficiently and equally well. That of BRL42715 appeared to be a factor of ten lower than that of the above two, but it showed the strongest β-lactamase inhibitory activity. This is most likely due to its better β-lactamase inactivating activity. BRL42715 at 1.56 μg ml −1 lowered the minimum inhibitory concentrations of ceftazidime and imipenem in a strain producing fully derepressed β-lactamase and an undetectable level of the outer membrane protein OprD2.
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