Literature DB >> 3258859

Comparison of glycine enhancement with cefoxitin induction of class 1 beta-lactamase production in Enterobacter cloacae ATCC 13047.

B J Gatus1, S M Bell, A S Jimenez.   

Abstract

The presence of either glycine or cefoxitin in the growth medium resulted in an increase in the beta-lactamase activity of cultures of Enterobacter cloacae ATCC 13047. Although the beta-lactamases produced as a result of either glycine enhancement or cefoxitin induction were identical there were striking differences in the kinetics of beta-lactamase production. The increased production of beta-lactamase which resulted from enhancement by glycine occurred late in the growth cycle whereas, with cefoxitin induction, the maximum production of beta-lactamase occurred early in logarithmic-phase growth. After the peak activity was reached the beta-lactamase activity appeared to decline with both processes. However, the mechanism of the apparent fall in the intracellular beta-lactamase activity was different with glycine enhancement and cefoxitin induction. In glycine enhanced cultures the fall presumably was due to leakage of intracellular beta-lactamase into the culture medium whereas with cefoxitin induced cultures there was dilution of beta-lactamase activity by bacterial protein derived from an increase in cell numbers after the cessation of induction. High extra-cellular levels of beta-lactamase activity were observed in cultures enhanced by glycine, whereas little beta-lactamase activity was detected in the medium when the cultures were induced by cefoxitin. The findings demonstrate that there are considerable differences between glycine enhancement and cefoxitin induction, but a final mechanism common to both processes exists which results in the production of identical beta-lactamases by E. cloacae ATCC 13047.

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Year:  1988        PMID: 3258859     DOI: 10.1093/jac/21.2.163

Source DB:  PubMed          Journal:  J Antimicrob Chemother        ISSN: 0305-7453            Impact factor:   5.790


  6 in total

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Authors:  A C Ottolenghi; J A Ayala
Journal:  Antimicrob Agents Chemother       Date:  1991-11       Impact factor: 5.191

2.  Physiological studies of the regulation of beta-lactamase expression in Pseudomonas maltophilia.

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Journal:  J Bacteriol       Date:  1989-01       Impact factor: 3.490

3.  Rapid method for determining the beta-lactamase-inducing potency of drugs.

Authors:  H Mett; I Oberkirch; B Schacher
Journal:  Eur J Clin Microbiol Infect Dis       Date:  1988-10       Impact factor: 3.267

Review 4.  beta-Lactamases in laboratory and clinical resistance.

Authors:  D M Livermore
Journal:  Clin Microbiol Rev       Date:  1995-10       Impact factor: 26.132

5.  Detection of resistance due to inducible beta-lactamase in Enterobacter aerogenes and Enterobacter cloacae.

Authors:  T W Huber; J S Thomas
Journal:  J Clin Microbiol       Date:  1994-10       Impact factor: 5.948

6.  Peptidoglycan tripeptide content and cross-linking are altered in Enterobacter cloacae induced to produce AmpC beta-lactamase by glycine and D-amino acids.

Authors:  A C Ottolenghi; M Caparrós; M A de Pedro
Journal:  J Bacteriol       Date:  1993-03       Impact factor: 3.490

  6 in total

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