Please use this identifier to cite or link to this item:
http://hdl.handle.net/10553/49969
Title: | Overexpression system and biochemical profile of CTX-M-3 extended-spectrum β-lactamase expressed in Escherichia coli | Authors: | Perilli, Mariagrazia Ettorre, Daniela Segatore, Bernardetta Caporale, Bibiana Santis, Francesca De Pochetti, Giorgio Brigante, Gioconda Mazza, Fernando Tavìo, Marìa M. Amicosante, Gianfranco |
UNESCO Clasification: | 32 Ciencias médicas 320103 Microbiología clínica |
Keywords: | Klebsiella-Pneumoniae Enterobacteriaceae Enzyme Identification Proteins, et al |
Issue Date: | 2004 | Journal: | FEMS Microbiology Letters | Abstract: | An efficient over-expression system was developed for CTX-M-3 extended-spectrum-beta-lactamase. The recombinant enzyme was purified from 11 of culture to yield 22 mg of pure enzyme. The N-terminal amino acid sequence was determined to be NH2-QTADVQ... Determination of kinetic parameters with the purified CTX-M-3 revealed efficient hydrolysis of penicillins and cephalosporins, while ceftazidime and aztreonam were very poor substrates. Clavulanic acid, sulbactam and especially tazobactam inhibited the CTX-M-3 enzyme. | URI: | http://hdl.handle.net/10553/49969 | ISSN: | 0378-1097 | DOI: | 10.1016/j.femsle.2004.10.031 | Source: | FEMS Microbiology Letters[ISSN 0378-1097],v. 241, p. 229-232 |
Appears in Collections: | Artículos |
SCOPUSTM
Citations
2
checked on Nov 24, 2024
WEB OF SCIENCETM
Citations
2
checked on Nov 24, 2024
Page view(s)
77
checked on Oct 5, 2024
Google ScholarTM
Check
Altmetric
Share
Export metadata
Items in accedaCRIS are protected by copyright, with all rights reserved, unless otherwise indicated.