Biochemical Properties of a Penicillin Beta-Lactamase Mediated by R Factor from Bordetella bronchiseptica | Zendy

Satoshi Yaginuma | Zendy; Nobuyuki Terakado | Zendy; Susumu Mitsuhashi | Zendy

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Biochemical Properties of a Penicillin Beta-Lactamase Mediated by R Factor from Bordetella bronchiseptica

Author(s) -

Satoshi Yaginuma,

Nobuyuki Terakado,

Susumu Mitsuhashi

Publication year - 1975

Publication title -

antimicrobial agents and chemotherapy

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.07

H-Index - 259

eISSN - 1070-6283

pISSN - 0066-4804

DOI - 10.1128/aac.8.3.238

Subject(s) - bordetella bronchiseptica , isoelectric point , benzylpenicillin , enzyme , isoelectric focusing , chemistry , chromatography , sephadex , penicillin , column chromatography , biochemistry , microbiology and biotechnology , enzyme assay , biology , bacteria , antibiotics , genetics

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.

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