The Aeromonas hydrophila CphA metallo-β-lactamase was overexpressed in a soluble secreted form in Escherichia coli using a T7 RNA polymerase-based expression system, and a simple protocol based on a single cation-exchange chromatographic step was developed, which is suitable for rapid purification of the overexpressed enzyme from E. coli lysates. A yield of up to 30 μg of purified enzyme per milliliter of culture was obtained. The purified enzyme preparation showed properties identical to those previously reported in the literature.
Hernandez Villadares, M., Galleni, M., Frère, J.M., Felici, A., Perilli, M., Franceschini, N., et al. (1996). Overproduction and purification of the Aeromonas hydrophila CphA metallo-beta-lactamase expressed in Escherichia coli. MICROBIAL DRUG RESISTANCE, 2(253), 256-256 [10.1089/mdr.1996.2.253].
Overproduction and purification of the Aeromonas hydrophila CphA metallo-beta-lactamase expressed in Escherichia coli
Rossolini G. M.;
1996-01-01
Abstract
The Aeromonas hydrophila CphA metallo-β-lactamase was overexpressed in a soluble secreted form in Escherichia coli using a T7 RNA polymerase-based expression system, and a simple protocol based on a single cation-exchange chromatographic step was developed, which is suitable for rapid purification of the overexpressed enzyme from E. coli lysates. A yield of up to 30 μg of purified enzyme per milliliter of culture was obtained. The purified enzyme preparation showed properties identical to those previously reported in the literature.
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https://hdl.handle.net/11365/29046
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