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PMID: 241286 Published · ppublish English Journal Article

Biochemical properties of a penicillin beta-lactamase mediated by R factor from Bordetella bronchiseptica.

Antimicrobial agents and chemotherapy ·Vol. 8 ·No. 3 ·1975-09-00 ·Pages 238-42

Yaginuma S, Terakado N, Mitsuhashi S

Abstract

The beta-lactamase specified by an R(te16) plasmid in Bordetella bronchiseptica was purified 200-fold by carboxymethyl-Sephadex column chromatography and electrofocusing. The enzyme has a molecular weight of 46,000 +/- 3,000 and an isoelectric point of 8.3 and was highly active against phenethicillin, oxacillin, and propicillin. The enzyme activity was inhibited by sodium chloride but not by ferrous ion. The maximal enzyme activity to benzylpenicillin was observed at pH 7.0 to 7.5 and at 40 C. It is concluded that this enzyme is different from the R-mediated beta-lactamases, i.e., the type I and type II beta-lactamases which have been classified in previous papers.

MeSH Terms
Bacterial Proteins/metabolism Bordetella/enzymology Drug Resistance, Microbial Electrophoresis, Agar Gel Hydrogen-Ion Concentration Isoelectric Focusing Kinetics Molecular Weight Penicillinase/isolation & purification,metabolism R Factors Temperature beta-Lactamase Inhibitors
Chemicals
Bacterial Proteins beta-Lactamase Inhibitors Penicillinase
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Yaginuma S
Terakado N
Mitsuhashi S
References (16)
16 references, click to expand
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Article Info
Journal
Antimicrobial agents and chemotherapy
Abbr.
Antimicrob Agents Chemother
ISSN
0066-4804
DOI
10.1128/AAC.8.3.238
Published
1975-09-00
Pages
238-42
Language
English
Region
United States
NLM ID
0315061
PMCID
PMC429300
Subset
IM
External Links
PubMed source DOI: 10.1128/AAC.8.3.238 PMC Full Text View journal details
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