Abstract
A penicillin beta-lactamase was purified from a strain of Alcaligenes dentrificans subsp. xylosoxydans resistant to beta-lactam antibiotics. The purified enzyme preparation gave a single protein band on polyacrylamide gel electrophoresis, and its molecular weight was 18,000 from sodium dodecylsulphate-acrylamide gel electrophoresis and gel filtration. Its isoelectric point was 9.8, the optimal pH was 8.5 and the optimal temperature was 35 degrees C. The enzyme hydrolyzed penicillin G and ampicillin more rapidly than cephalosporins. Relative rates, with penicillin G as 100, were: ampicillin, 102; carbenicillin, 15; cloxacillin, less than 1; piperacillin, 9; cephaloridine, 41; cefoperazone, 36; cefpiramide, 36 and cefmenoxime, 14. Clavulanic acid, sulbactam, imipenem, and cephamycins had low affinities for the enzyme. The enzyme activity was inhibited by iodine, Hg2+, clavulanic acid and sulbactam.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
