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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