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PMID: 4942446 Published · ppublish English Journal Article

The purification and properties of the -lactamase specified by the resistance factor R-1818 in Escherichia coli and Proteus mirabilis.

The Biochemical journal ·Vol. 123 ·No. 4 ·1971-07-00 ·Pages 493-500

Dale JW, Smith JT

Abstract

1. The beta-lactamase specified by the R-1818 resistance factor in Escherichia coli was purified 300-fold; the resulting preparation gave a single peak on Sephadex G-100 and a single band on polyacrylamide-gel electrophoresis. 2. The beta-lactamase specified by the same R-factor in Proteus mirabilis was purified over 2000-fold, but was still far from pure. The specific activity of this preparation was one-fifth that of the purified enzyme from E. coli. 3. The two enzymes were shown to be identical as regards substrate specificity, pH optimum, K(m) values and molecular weight. 4. It is suggested that the low beta-lactamase activity of extracts of P. mirabilis (R-1818), about 5% of that from E. coli (R-1818) in crude extracts, could be due to inefficient transcription of the R-factor DNA by Proteus RNA polymerase.

MeSH Terms
Chromatography, Gel DNA, Bacterial Electrophoresis, Disc Escherichia coli/enzymology Genetic Code Hydrogen-Ion Concentration Kinetics Molecular Weight Penicillin Resistance Penicillinase/isolation & purification,metabolism Proteus/enzymology RNA Nucleotidyltransferases
Chemicals
DNA, Bacterial RNA Nucleotidyltransferases Penicillinase
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Dale J W
Smith J T
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27 references, click to expand
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
Published
1971-07-00
Pages
493-500
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1176988
Subset
IM
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