Open AccessEnzymatic and Immunological Characterization of a New Cephalosporinase from Enterobacter aerogenes
Author(s) -
Robert Letarte,
Marlyse Devaud-Felix,
Jean-Claude Péchère,
Diane Allard-Leprohon
Publication year - 1977
Publication title -
antimicrobial agents and chemotherapy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.07
H-Index - 259
eISSN - 1070-6283
pISSN - 0066-4804
DOI - 10.1128/aac.12.2.201
Subject(s) - enterobacter aerogenes , enterobacter cloacae , cephalosporin , carbenicillin , enterobacter , microbiology and biotechnology , penicillin , enzyme , benzylpenicillin , ampicillin , isoelectric point , chemistry , cefotiam , cefotaxime , chromatography , enterobacteriaceae , biochemistry , biology , escherichia coli , antibiotics , gene
A hospital strain ofEnterobacter aerogenes (MULB 250) isolated from a urinary tract infection was found to be cephalosporin and ampicillin resistant and carbenicillin susceptible. The β-lactamase produced by this strain was extracted and purified by means of affinity chromatography, using a cephalosporin C-bound Sepharose 4B column. The purified enzyme was tested for hydrolysis of penicillin and various cephalosporins. TheKm value is 11.8 μM for benzyl penicillin and 130 μM for cephalosporin C. The isoelectric point of the enzyme is 9.3, and its molecular weight is 29,500 ± 1,000. Rabbit antiserum obtained against this MULB 250 β-lactamase showed no cross-reaction with other penicillinases or cephalosporinases in neutralization tests. Comparisons of results obtained with other β-lactamases, particularly fromEnterobacter cloacae P99, indicate that theEnterobacter MULB 250 enzyme presents a typical cephalosporinase profile. As far as we know, this type of enzyme is relatively rare.
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