Improved purification and characterization of the OXA-2 β-lactamase
- 15 December 1984
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 224 (3) , 1009-1013
- https://doi.org/10.1042/bj2241009
Abstract
An improved and scaled-up procedure has been developed for purifying the OXA-2 plasmid-mediated beta-lactamase. This has enabled us to improve the characterization of this enzyme, including a revised determination of its amino acid composition and the sequence of the N-terminal region of the protein.This publication has 24 references indexed in Scilit:
- A direct spectrophotometric assay and determination of Michaelis constants for the β-lactamase reactionAnalytical Biochemistry, 1975
- R-factor-mediated beta-lactamases that hydrolyze oxacillin: evidence for two distinct groups.1974
- A new acid hydrolysis method for determining tryptophan in peptides and proteinsAnalytical Biochemistry, 1974
- Maturation of the head of bacteriophage T4Journal of Molecular Biology, 1973
- Characterization of the β-lactamase specified by the resistance factor R-1818 in Escherichia coli K12 and other Gram-negative bacteriaBiochemical Journal, 1971
- The purification and properties of the β-lactamase specified by the resistance factor R-1818 in Escherichia coli and Proteus mirabilisBiochemical Journal, 1971
- The Reliability of Molecular Weight Determinations by Dodecyl Sulfate-Polyacrylamide Gel ElectrophoresisJournal of Biological Chemistry, 1969
- Circular DNA forms of colicinogenic factors E1, E2 and E3 from Escherichia coliJournal of Molecular Biology, 1968
- The relation of resistance transfer factors to the F-factor (sex-factor) ofEscherichia coliK12Genetics Research, 1966
- RESISTANCE TO PENICILLINS AND ITS TRANSFER IN ENTEROBACTERIACEÆThe Lancet, 1965