The β-lactamase stability of amoxycillin with the β-lactamase inhibitor, clavulanic acid
- 1 January 1983
- journal article
- research article
- Published by Oxford University Press (OUP) in Journal of Antimicrobial Chemotherapy
- Vol. 11 (1) , 27-32
- https://doi.org/10.1093/jac/11.1.27
Abstract
The stability of low concentrations of amoxycillin in the presence of clavulanic acid (potassium salt) was determined for a wide range of clinically important β-lactamases including the staphylococcal and TEM plasmid mediated enzymes. Even with enzyme preparations which completely hydrolysed the amoxycillin within a minute, clavulanic acid provided significant protection. The time course of the protection of amoxycillin reflected the time dependent action of clavulanic acid.Keywords
This publication has 5 references indexed in Scilit:
- The inhibition of β-lactamases from Gram-negative bacteria by clavulanic acidBiochemical Journal, 1981
- The inhibition of staphylococcal β-lactamase by clavulanic acidBiochemical Journal, 1979
- Chemical studies on the inactivation of Escherichia coli RTEM β-lactamase by clavulanic acidBiochemistry, 1978
- Kinetic studies on the inactivation of Escherichia coli RTEM β-lactamase by clavulanic acidBiochemistry, 1978
- Clavulanic Acid: a Beta-Lactamase-Inhibiting Beta-Lactam from Streptomyces clavuligerusAntimicrobial Agents and Chemotherapy, 1977