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PMID: 5328167 Published · ppublish English Journal Article

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

The Biochemical journal ·Vol. 98 ·No. 1 ·1966-01-00 ·Pages 204-9

Datta N, Richmond MH

Abstract

1. The penicillinase (beta-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.

MeSH Terms
Cephalosporins/metabolism Chemical Phenomena Chemistry Chromatography, Gel Enterobacter/enzymology Escherichia coli/enzymology Genes In Vitro Techniques Molecular Biology Penicillinase/metabolism Penicillins/metabolism
Chemicals
Cephalosporins Penicillins Penicillinase
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Datta N
Richmond M H
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25 references, click to expand
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
DOI
10.1042/bj0980204
Published
1966-01-00
Pages
204-9
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1264816
Subset
IM
External Links
PubMed source DOI: 10.1042/bj0980204 PMC Full Text View journal details
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