Non-inducible, mainly cell-associated β-lactamase from Nocardia asteroides strain 108

The beta-lactamase of the soil-borne strain 108 (parental strain) of Nocardia asteroides is a non-inducible enzyme mainly associated with the cells; it can be efficiently extracted by ultrasonication and SDS treatment. Crude enzyme preparations showed penicillinase and cephalosporinase activity. The...

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Veröffentlicht in:Journal of antimicrobial chemotherapy 1997-07, Vol.40 (1), p.5-11
Hauptverfasser: SCOPETTI, F, FATTORINI, L, FRANCESCHINI, N, AMICOSANTE, G, OREFICI, G
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container_end_page 11
container_issue 1
container_start_page 5
container_title Journal of antimicrobial chemotherapy
container_volume 40
creator SCOPETTI, F
FATTORINI, L
FRANCESCHINI, N
AMICOSANTE, G
OREFICI, G
description The beta-lactamase of the soil-borne strain 108 (parental strain) of Nocardia asteroides is a non-inducible enzyme mainly associated with the cells; it can be efficiently extracted by ultrasonication and SDS treatment. Crude enzyme preparations showed penicillinase and cephalosporinase activity. The kinetics of beta-lactamase production and in-vitro susceptibility to combinations of beta-lactam antibiotics plus beta-lactamase inhibitors have been studied in two stable overproducer mutants (A14 and B1) obtained by mutagenization of the parental strain with nitrosoguanidine. The cell-associated enzyme increased with bacterial growth in parental and mutant strains and was particularly abundant in stationary phase cells. The beta-lactamase inhibitors sulbactam and clavulanic acid decreased MIC values of penicillins more efficiently in the parental strain than in mutants, thus indicating some involvement of the enzyme in the resistance of N. asteroides strain 108 to beta-lactam antibiotics.
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Crude enzyme preparations showed penicillinase and cephalosporinase activity. The kinetics of beta-lactamase production and in-vitro susceptibility to combinations of beta-lactam antibiotics plus beta-lactamase inhibitors have been studied in two stable overproducer mutants (A14 and B1) obtained by mutagenization of the parental strain with nitrosoguanidine. The cell-associated enzyme increased with bacterial growth in parental and mutant strains and was particularly abundant in stationary phase cells. 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Crude enzyme preparations showed penicillinase and cephalosporinase activity. The kinetics of beta-lactamase production and in-vitro susceptibility to combinations of beta-lactam antibiotics plus beta-lactamase inhibitors have been studied in two stable overproducer mutants (A14 and B1) obtained by mutagenization of the parental strain with nitrosoguanidine. The cell-associated enzyme increased with bacterial growth in parental and mutant strains and was particularly abundant in stationary phase cells. 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subjects Amoxicillin - pharmacology
Bacteriology
beta-Lactam Resistance - physiology
beta-Lactamases - drug effects
beta-Lactamases - genetics
beta-Lactamases - metabolism
beta-Lactams - metabolism
beta-Lactams - pharmacology
Biological and medical sciences
Cefoxitin - pharmacology
Detergents - pharmacology
Fundamental and applied biological sciences. Psychology
Hydrolysis
Isoelectric Point
Microbiology
Mutagenesis
Mutation
Nocardia asteroides
Nocardia asteroides - drug effects
Nocardia asteroides - enzymology
Nocardia asteroides - genetics
Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains
Penicillin G - pharmacology
title Non-inducible, mainly cell-associated β-lactamase from Nocardia asteroides strain 108
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