Effect of Piperacillin on D-Alanine Carboxypeptidase Activities from Pseudomonas aeruginosa
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چکیده
منابع مشابه
Effect of subinhibitory concentration of piperacillin/tazobactam on Pseudomonas aeruginosa.
Subinhibitory concentrations (sub-MICs) of antibiotics, although not able to kill bacteria, can modify their physico-chemical characteristics and the architecture of their outermost surface and may interfere with some bacterial functions. This study investigated the ability of sub-MIC piperacillin/tazobactam (P/T) to interfere with the bacterial virulence parameters of adhesiveness, cell-surfac...
متن کاملD=Alanine Carboxypeptidase from Bacillus subtilis Membranes
The D-alanine carboxypeptidase was solubilized from the membranes of Bacillus subtilis with the nonionic detergent, Triton X-100, and pursed to homogeneity. The purified protein bound irreversibly radioactivity from [Wlpenicillin G. It contained a single polypeptide chain of molecular weight 50,000 and existed in solution as a protein-detergent aggregate of molecular weight about 350,000. The a...
متن کاملEffect of Subinhibitory concentrations of imipenem and piperacillin on transcriptional expression of algD and lasB genes in Pseudomonas aeruginosa
Sub Minimal Inhibitory concentrations (sub-MIC) of antibiotics, although not able to kill bacteria, can be effect on their physico- chemical characteristics and functions. This study aimed to investigate the effect of sub-MIC of imipenem and piperacillin on the transcriptional expression of virulence related genes algD and lasB in Pseudomonas auroginosa. Five clinical isolates of P. aeruginosa ...
متن کاملMutation in Pseudomonas aeruginosa causing simultaneous defects in penicillin-binding protein 5 and in enzyme activities of penicillin release and D-alanine carboxypeptidase.
Penicillin-binding protein 5 in Pseudomonas aeruginosa had moderately penicillin-sensitive D-alanine carboxypeptidase activity. As in Escherichia coli, a defect in this enzyme activity was not lethal.
متن کاملDD-carboxypeptidase and peptidoglycan transpeptidase from Pseudomonas aeruginosa.
Peptidoglycan transpeptidase and dd-carboxypeptidase have been detected in isolated membranes of Pseudomonas aeruginosa. Cephalosporins and penicillins fail to inhibit the transpeptidase at concentrations as high as 100 mug/ml. dd-Carboxypeptidase, on the other hand, is sensitive to inhibition by beta-lactam antibiotics. The presence of dimethyl sulfoxide in the reaction mixture results in a tw...
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ژورنال
عنوان ژورنال: Journal of General Microbiology
سال: 1979
ISSN: 0022-1287
DOI: 10.1099/00221287-112-1-181