Lincomycin stimulates synthesis of TEM-2 beta-lactamase by Escherichia coli

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Lincomycin stimulates synthesis of TEM-2 beta-lactamase by Escherichia coli.

Lincomycin increased the TEM-2 beta-lactamase activity of Escherichia coli K-12 cells carrying plasmid RP4 at a concentration which slightly inhibited cell growth. In a control culture beta-lactamase activity reached its maximal level in late log phase, whereas when lincomycin was present beta-lactamase activity continued to increase into the stationary phase. Lincomycin (100 micrograms/ml) inh...

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Effects of lincomycin on synthesis of TEM beta-lactamase by Escherichia coli.

Sub-inhibitory concentrations of lincomycin slightly inhibit growth of Escherichia coli carrying plasmid RP4 and cause a 2-fold increase in TEM-2 beta-lactamase. To analyze this effect, cultures were pulse-labeled with [3H]leucine, chased with non-radioactive leucine and immunoprecipitated with anti-beta-lactamase antiserum. The synthesis rate of beta-lactamase was two times higher in inhibited...

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Lytic Activity of Isolated Phage from Milk Against Extended-Spectrum Beta-Lactamase Escherichia coli

 Background and purpose: Escherichia coli (E.coli) is the most common cause of urinary tract infection. The treatment strategy has been hampered by the emergence of broad-spectrum beta-lactamase-producing E.coli and its resistance to most antibiotics. Bacteriophages are suggested as an alternative treatment option. This study aimed at evaluating the lytic activity of isolated phage from unpaste...

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Fecal carriage of Escherichia coli harboring extended-spectrum beta-lactamase (ESBL) genes by sheep and broilers in Urmia region, Iran

Background: There is a growing concern on the impact of the presence of extended-spectrum β-lactamase (ESBL) producing Escherichia coli isolated from animals on public health. OBJECTIVES: The aim of this study was to investigate the presence of three classes of ESBL genes in E. coli isolates from sheep and broilers at a slaughter in Urmia region, Iran. METHODS: A total of 111 E. coli isolates w...

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Purification of TEM-1 beta-lactamase by immunoaffinity chromatography.

A monoclonal antibody prepared against TEM-1 beta-lactamase was found to compete with penicillins and cephalosporins for binding to the enzyme. The purified antibody preparation was linked to Sepharose 4B and used for immunoaffinity-chromatography purification of TEM-1 beta-lactamase. Elution with either benzylpenicillin or cloxacillin yielded a highly purified, concentrated and active enzyme p...

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ژورنال

عنوان ژورنال: Antimicrobial Agents and Chemotherapy

سال: 1986

ISSN: 0066-4804,1098-6596

DOI: 10.1128/aac.30.1.82