| Literature DB >> 9158768 |
M Hernandez Villadares1, M Galleni, J M Frère, A Felici, M Perilli, N Franceschini, G M Rossolini, A Oratore, G Amicosante.
Abstract
The Aeromonas hydrophila CphA metallo-beta-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 micrograms of purified enzyme per milliliter of culture was obtained. The purified enzyme preparation showed properties identical to those previously reported in the literature.Entities:
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Year: 1996 PMID： 9158768 DOI： 10.1089/mdr.1996.2.253
Source DB: PubMed Journal: Microb Drug Resist ISSN： 1076-6294 Impact factor: 3.431