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Characterisation of CMY-4, an AmpC-type plasmid-mediated β-lactamase in a Tunisian clinical isolate of Proteus mirabilis (1998)

Verdet, Charlotte ; Arlet, Guillaume ; Redjeb, Saida Ben ; [et al.]

Oxford, UK : Blackwell Publishing Ltd

FEMS microbiology letters 169 (1998), S. 0

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ISSN: 1574-6968

Source: Blackwell Publishing Journal Backfiles 1879-2005

Topics: Biology

Notes: A strain of Proteus mirabilis resistant to β-lactams, including cefoxitin, was isolated from the urine of a woman from Tunisia. Its antibiotic susceptibility pattern and that of the Escherichia coli transconjugant suggested the presence of an AmpC-type β-lactamase. Two bands of β-lactamase activity (pI 5.4 and 9.2) were detected by isoelectric focusing. The nucleotide sequence of the gene encoding the AmpC-type enzyme was determined. The deduced amino acid sequence was 98–99% identical to CMY-3 and to those of the plasmid-mediated AmpC-type β-lactamases originated from Citrobacter freundii and 97% identical to the chromosome-encoded β-lactamase of a Tunisian clinical isolate of C. freundii. This enzyme differs from CMY-2 by one substitution (Arg for Trp at position 221) and from CMY-3 by two substitutions (Glu for Gly at position 42 and Ser for Asn at position 363) and we propose the denomination CMY-4.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1111/j.1574-6968.1998.tb13323.x

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Voltammetric method for the determination of H2O2 in rainwater (1991)

Lagrange, Janine ; Lagrange, Philippe

Springer

Fresenius' Zeitschrift für analytische Chemie 339 (1991), S. 452-454

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ISSN: 1618-2650

Source: Springer Online Journal Archives 1860-2000

Topics: Chemistry and Pharmacology

Notes: Summary Presented below is an electrochemical method for the determination of hydrogen peroxide levels in the atmospheric liquid water. The hydrogen peroxide concentration is determined by a voltammetric method involving a rotating disk electrode. The oxidation limiting current at +0.4 V/SCE is proportional to the concentration of hydrogen peroxide found in 1 mol/l KNO3 containing a phosphate buffer, pH 7.5. An analytical blank is prepared ‘in situ’ by addition of catalase enzyme to avoid interferences. The detection limit obtained is 5×10−9 mol/l.