These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Comparison of glycine enhancement with cefoxitin induction of class 1 beta-lactamase production in Enterobacter cloacae ATCC 13047.
    Author: Gatus BJ, Bell SM, Jimenez AS.
    Journal: J Antimicrob Chemother; 1988 Feb; 21(2):163-70. PubMed ID: 3258859.
    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.
    [Abstract] [Full Text] [Related] [New Search]