The IMP-13 metallo-beta-lactamase was overproduced in Escherichia coli BL21(DE3) and purified by chromatography. Analysis of kinetic parameters revealed some notable differences with other IMP-type enzymes, noteworthily a higher catalytic efficiency toward ticarcillin and piperacillin and a marked preference for imipenem over meropenem.

Santella, G., Docquier, J.D., Gutkind, G., Rossolini, G.M., Radice, M. (2011). Purification and biochemical characterization of IMP-13 metallo-beta-lactamase. ANTIMICROBIAL AGENTS AND CHEMOTHERAPY, 55(1), 399-401 [10.1128/AAC.00421-10].

Purification and biochemical characterization of IMP-13 metallo-beta-lactamase.

DOCQUIER, JEAN DENIS;ROSSOLINI, GIAN MARIA;
2011-01-01

Abstract

The IMP-13 metallo-beta-lactamase was overproduced in Escherichia coli BL21(DE3) and purified by chromatography. Analysis of kinetic parameters revealed some notable differences with other IMP-type enzymes, noteworthily a higher catalytic efficiency toward ticarcillin and piperacillin and a marked preference for imipenem over meropenem.
2011
Santella, G., Docquier, J.D., Gutkind, G., Rossolini, G.M., Radice, M. (2011). Purification and biochemical characterization of IMP-13 metallo-beta-lactamase. ANTIMICROBIAL AGENTS AND CHEMOTHERAPY, 55(1), 399-401 [10.1128/AAC.00421-10].
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11365/20972
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