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PMID: 900918 Published · ppublish English Journal Article

Enzymatic and immunological characterization of a new cephalosporinase from Enterobacter aerogenes.

Antimicrobial agents and chemotherapy ·Vol. 12 ·No. 2 ·1977-08-00 ·Pages 201-5

Letarte R, Devaud-Felix M, Pechere JC, Allard-Leprohon D

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 beta-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 muM for benzyl penicillin and 130 muM 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 beta-lactamase showed no cross-reaction with other penicillinases or cephalosporinases in neutralization tests. Comparisons of results obtained with other beta-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.

MeSH Terms
Amidohydrolases/isolation & purification Antibody Specificity Cephalosporinase/immunology,isolation & purification,metabolism Chromatography, Affinity Drug Resistance, Microbial Enterobacter/enzymology Enterobacteriaceae/enzymology Isoelectric Focusing Kinetics Molecular Weight
Chemicals
Amidohydrolases Cephalosporinase
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Letarte R
Devaud-Felix M
Pechere J C
Allard-Leprohon D
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25 references, click to expand
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Article Info
Journal
Antimicrobial agents and chemotherapy
Abbr.
Antimicrob Agents Chemother
ISSN
0066-4804
Published
1977-08-00
Pages
201-5
Language
English
Region
United States
NLM ID
0315061
PMCID
PMC429885
Subset
IM
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