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. 1976 Jan;9(1):55–60. doi: 10.1128/aac.9.1.55

Plasmid-Mediated Penicillin Beta-Lactamases in Pseudomonas aeruginosa

Yosuke Sawada 1, Satoshi Yaginuma 1, Masaru Tai 1, Shizuko Iyobe 1, Susumu Mitsuhashi 1
PMCID: PMC429473  PMID: 4010

Abstract

A penicillin β-lactamase (PCase) was extracted from Pseudomonas aeruginosa Rms139+ and purified by means of column chromatography. The isoelectric point of Rms139 PCase was 5.7 and its molecular weight was 22,500 ± 1,000. The optimal pH for the hydrolysis of benzylpenicillin was 7.0 to 7.5 and the optimal temperature was 45 C, with the PCase also showing high activity against carbenicillin. It is concluded that this enzyme is a new type of penicillin β-lactamase different from the type I, II, or III R plasmid-mediated PCases reported previously.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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