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Chloramphenicol acetyltransferase of bacteroides-fragilis


Britz, ML and Wilkinson, RG, Chloramphenicol acetyltransferase of bacteroides-fragilis, Antimicrobial Agents and Chemotherapy, 14, (1) pp. 105-111. ISSN 0066-4804 (1978) [Refereed Article]

DOI: doi:10.1128/AAC.14.1.105


Chloramphenicol-resistant strains of B. fragilis (minimum inhibitory concentration, 12.5 μg/ml) were isolated from a stool specimen which contained multiply resistant Escherichia coli. The enzyme responsible for resistance, chloramphenicol acetyltransferase, was produced constitutively by these strains; the specific activity was 10-fold lower than that of the E. coli enzymes. Similar activity was not detected in susceptible B. fragilis strains, nor could it be induced by growth in the presence of chloramphenicol or by mutagenesis. The enzyme had a pH optimum of 7.8 and a molecular weight of approximately 89,000. The Km for chloramphenicol was 5.2 μM, and the enzyme was sensitive to inhibition by 5.5'-dithiobis-2-nitrobenzoic acid. The enzyme produced by an E. coli strain isolated from the same specimen had a similar Km and sensitivity to 5.5'-dithiobis-2-nitrobenzoic acid.

Item Details

Item Type:Refereed Article
Research Division:Biological Sciences
Research Group:Microbiology
Research Field:Bacteriology
Objective Division:Health
Objective Group:Clinical health
Objective Field:Clinical health not elsewhere classified
UTAS Author:Britz, ML (Professor Margaret Britz)
ID Code:73229
Year Published:1978
Web of Science® Times Cited:51
Deposited By:Research Division
Deposited On:2011-09-22
Last Modified:2011-09-22

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