Frequency of β-lactamases that are markedly active against carbenicillin in the Pseudomonas aeruginosa strains isolated in a Medical School Hospital
- 1 January 1983
- journal article
- research article
- Published by Oxford University Press (OUP) in Journal of Antimicrobial Chemotherapy
- Vol. 12 (5) , 451-458
- https://doi.org/10.1093/jac/12.5.451
Abstract
During 1 yr 71 carbenicillin-resistant P. aeruginosa strains were isolated. The detection of the .beta.-lactamase activity in these strains was performed by the iodometric method. The .beta.-lactamases were found in 70% of the carbenicillin-resistant strains and were characterized by isoelectric focusing and by determination of substrate profiles. Of the .beta.-lactamases tested, 72% focused in the same way as the PSE-1 type from strain PU21(RPL11). The determination of the substrate profiles by the acidimetric method showed that these enzymes had a high activity towards carbenicillin and that they can vary in their hydrolysis of cephalosporins. Such PSE-1 type .beta.-lactamases were found in gentamicin-tobramycin-resistant strains; other types of enzymes (PSE-4 enzymes and enzymes with pI 7.7) were found in strains sensitive to these antibiotics.This publication has 5 references indexed in Scilit:
- Spread of a "Pseudomonas-specific" beta-lactamase to plasmids of enterobacteriaJournal of Bacteriology, 1982
- Properties of three carbenicillin-hydrolysing β-lactamases (CARB) from Pseudomonas aeruginosa: identification of a new enzymeJournal of Antimicrobial Chemotherapy, 1981
- Screening methods for detection of β-lactamases in Gram-negative bacteriaJournal of Antimicrobial Chemotherapy, 1979
- Cephalosporinase and penicillinase activities of a β-lactamase from Pseudomonas pyocyaneaBiochemical Journal, 1965
- Staphylococcal penicillinase and the new penicillinsBiochemical Journal, 1962