Affiliation:
1. Department of Microbiology, Faculty of Medicine, Laval University, Quebec, Canada, G1K 7P4
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
K
m
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.
Publisher
American Society for Microbiology
Subject
Infectious Diseases,Pharmacology (medical),Pharmacology
Cited by
19 articles.
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