Detection of Hydrolysis of ß-Lactam Substrate by TEM-1 Enzyme and Inhibitor Binding using the FlexStation® 3 Microplate Reader

This application note reports the use of the FlexStation^® 3 system in determining the binding affinity of ß-lactamase inhibitory protein (BLIP) to TEM-1. Bacterial resistance to ß-lactam drugs through the production of class A ß-lactamase enzymes is an increasing concern in the medical community. BLIP produced by the soil bacterium Streptomyces clavuligeris inhibits a number of class A ß-lactamases with a wide range of affinities, thereby restoring the effectiveness of life-saving antibiotics.