Purification and properties of two extracellular beta-lactamases from Bacillus cereus 569-H
- PMID: 4990588
- PMCID: PMC1179213
- DOI: 10.1042/bj1180457
Purification and properties of two extracellular beta-lactamases from Bacillus cereus 569-H
Abstract
1. When Bacillus cereus 569/H was grown in a casamino acid (casein-hydrolysate) medium containing zinc sulphate rapid production of extracellular beta-lactamase II preceded that of beta-lactamase I. 2. beta-Lactamase I was separated from beta-lactamase II by fractional precipitation with ammonium sulphate. 3. beta-Lactamase I was purified by a process involving chromatography on Celite and DEAE-cellulose and beta-lactamase II by chromatography on DEAE-cellulose after denaturation of beta-lactamase I by heat. Both enzymes were obtained in crystalline form. 4. beta-Lactamase II prepared in this way appeared to have a higher molecular weight than beta-lactamase I and required Zn(2+) as a cofactor for both cephalosporinase and penicillinase activities.
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