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. 1966 Jan;98(1):204–209. doi: 10.1042/bj0980204

The purification and properties of a penicillinase whose synthesis is mediated by an R-factor in Escherichia coli

Naomi Datta 1,2, M H Richmond 1,2,*
PMCID: PMC1264816  PMID: 5328167

Abstract

1. The penicillinase (β-lactamase) from Escherichia coli strain TEM has been purified and its activity against a range of penicillin and cephalosporin derivatives measured. 2. The enzyme shows little resemblance to penicillinases from Bacillus cereus, Bacillus licheniformis and Staphylococcus aureus. 3. The molecular weight of the enzyme is 16700±5%, which is about half the value obtained for other penicillinases. 4. The enzyme is most similar in properties to a crude preparation of a penicillinase from Klebsiella (Aerobacter) aerogenes, but clearly different from crude enzyme preparations from other strains of E. coli. 5. Since penicillinase synthesis in E. coli strain TEM is mediated by an R-factor known to infect many other species of Enterobacteriaceae, the appearance of similar enzymes in other Gramnegative species is not surprising.

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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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