Enzymatic and Immunological Characterization of a New Cephalosporinase from Enterobacter aerogenes |
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Authors: | Robert Letarte Marlyse Devaud-Felix Jean-Claude Pechere and Diane Allard-Leprohon |
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Institution: | 1.Department of Microbiology, Faculty of Medicine, Laval University, Quebec, Canada, G1K 7P4 |
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Abstract: | A hospital strain of Enterobacter 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. The Km 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 from Enterobacter cloacae P99, indicate that the Enterobacter MULB 250 enzyme presents a typical cephalosporinase profile. As far as we know, this type of enzyme is relatively rare. |
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