Abstract
The β-lactamase from Escherichia coli ML 4953 pKU56 was purified about 190-fold from the crude cell-free extract with an overall recovery of 17%. The molecular weight mediated by pKU56 was about 28,000, and the isoelectric point was about 9.4. This enzyme hydrolyzed cephaloridine, cephalothin, cefamandole, cefuroxime, and cefsulodin at high rate, but ampicillin, piperacillin, and carbenicillin moderately. Antisera against pKU56 enzyme showed partly cross-reaction with β-lactamase from Klebsiella oxytoca and Proteus vulgaris.
Original language | English |
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Pages (from-to) | 70-72 |
Number of pages | 3 |
Journal | Journal of Infection and Chemotherapy |
Volume | 1 |
Issue number | 1 |
DOIs | |
Publication status | Published - 1995 Jan 1 |
Keywords
- extended-spectrum
- pKU56
- β-lactamase
ASJC Scopus subject areas
- Microbiology (medical)
- Pharmacology (medical)
- Infectious Diseases