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PMID: 6609682 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Purification and properties of an inducible cephalosporinase from Pseudomonas maltophilia GN12873.

Antimicrobial agents and chemotherapy ·Vol. 25 ·No. 3 ·1984-03-00 ·Pages 362-5

Saino Y, Inoue M, Mitsuhashi S

Abstract

An inducible cephalosporinase was purified from Pseudomonas maltophilia GN12873. The pI was 8.4, and the molecular weight was ca. 56,000 by gel filtration or 27,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, suggesting that this enzyme had two subunits. The optimal pH and optimal temperature were 7.5 and 45 degrees C, respectively. Enzyme activity was inhibited by clavulanic acid, sulbactam, cephamycin derivatives, carbapenem antibiotics, iodine, HgCl2, and p-chloromercuribenzoate. The enzyme showed a broad substrate profile, hydrolyzing cephaloridine, cefazolin, cefsulodin, penicillin G, ceftizoxime, and ampicillin at a high rate.

MeSH Terms
Anti-Bacterial Agents/pharmacology Bacterial Proteins/isolation & purification Cephalosporinase/isolation & purification,metabolism Chemical Phenomena Chemistry, Physical Chromatography, Gel Enzyme Induction/drug effects Hydrogen-Ion Concentration Pseudomonas/enzymology beta-Lactamase Inhibitors beta-Lactamases/metabolism
Chemicals
Anti-Bacterial Agents Bacterial Proteins beta-Lactamase Inhibitors Cephalosporinase beta-Lactamases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Saino Y
Inoue M
Mitsuhashi S
References (18)
18 references, click to expand
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Article Info
Journal
Antimicrobial agents and chemotherapy
Abbr.
Antimicrob Agents Chemother
ISSN
0066-4804
Published
1984-03-00
Pages
362-5
Language
English
Region
United States
NLM ID
0315061
PMCID
PMC185518
Subset
IM
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