Investigation of the Interactions between β-Lactams and a Metallo-β-lactamase from Bacillus cereus Using a Monoclonal Antibody
✍ Scribed by S.J. Chambers; G.M. Wyatt; M.R.A. Morgan
- Publisher
- Elsevier Science
- Year
- 2001
- Tongue
- English
- Weight
- 175 KB
- Volume
- 288
- Category
- Article
- ISSN
- 0003-2697
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✦ Synopsis
A monoclonal antibody recognizing the active site of a -lactamase from Bacillus cereus was identified and characterized. The binding of the monoclonal antibody to the active site was quantitatively inhibited by a broad spectrum of -lactam antibiotics. The levels of inhibition were found to be associated with particular structural features of the antibiotics and their ability to form stable enzyme/substrate complexes. A novel, broad specificity assay for -lactams was developed based on the inhibition of antibody binding of all the -lactams studied. The assay is applicable to detection of -lactams at or close to the MRL level and would be complementary to existing receptor-based assays. The approach described is relevant to the study of kinetic aspects of -lactamases and could prove a useful tool in future drug development.