The beta-lactamase stability of amoxycillin with the beta-lactamase inhibitor, clavulanic acid.
The stability of low concentrations of amoxycillin in the presence of clavulanic acid (potassium salt) was determined for a wide range of clinically important beta-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.
D000658:Amoxicillin / Q000378:metabolism*; D002433:Cefaclor / Q000494:pharmacology; D002876:Chromosomes, Bacterial / Q000378:metabolism; D019818:Clavulanic Acid; D002969:Clavulanic Acids / Q000494:pharmacology*; D007700:Kinetics; D013211:Staphylococcus aureus / Q000201:enzymology; D013997:Time Factors; D065093:beta-Lactamase Inhibitors; D001618:beta-Lactamases / Q000378:metabolism*
D002969:Clavulanic Acids; D065093:beta-Lactamase Inhibitors; D019818:Clavulanic Acid; D002433:Cefaclor; D000658:Amoxicillin; D001618:beta-Lactamases