Clavulanic acid inhibition of .BETA.-lactamase I from Bacillus cereus 569/H.
- 1 January 1978
- journal article
- research article
- Published by Japan Antibiotics Research Association in The Journal of Antibiotics
- Vol. 31 (11) , 1162-1169
- https://doi.org/10.7164/antibiotics.31.1162
Abstract
Inactivation of .beta.-lactamase I by clavulanic acid was investigated. Clavulanic acid induced inhibition of the enzyme was progressive with time. Benzylpenicillin provided protection against the adverse effects of the inhibitor initially, but the enzyme was irreversibly inhibited in a progressive manner even in the presence of substrate. Reaction of .beta.-lactamase I with clavulanic acid, in the presence of ampicillin, led to a very rapid inactivation of the enzyme.This publication has 4 references indexed in Scilit:
- 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
- Production ofBacillus cereus exopenicillinase on a pilot-plant scaleBiotechnology & Bioengineering, 1965