CENTA, a chromogenic cephalosporin, is readily hydrolyzed by β-lactamases of all classes except for the Aeromonas hydrophila metalloenzyme. Although it cannot practically be used for the detection of β-lactamase-producing strains on agar plates, it should be quite useful for kinetic studies and the detection of the enzymes in crude extracts and chromatographic fractions.

Bebrone, C., Moali, C., Mahy, F., Rival, S., Docquier, J.D., Rossolini, G.M., et al. (2001). CENTA as a chromogenic substrate for studying β-lactamases. ANTIMICROBIAL AGENTS AND CHEMOTHERAPY, 45(6), 1868-1871 [10.1128/AAC.45.6.1868-1871.2001].

CENTA as a chromogenic substrate for studying β-lactamases

DOCQUIER, JEAN DENIS;ROSSOLINI, GIAN MARIA;
2001-01-01

Abstract

CENTA, a chromogenic cephalosporin, is readily hydrolyzed by β-lactamases of all classes except for the Aeromonas hydrophila metalloenzyme. Although it cannot practically be used for the detection of β-lactamase-producing strains on agar plates, it should be quite useful for kinetic studies and the detection of the enzymes in crude extracts and chromatographic fractions.
2001
Bebrone, C., Moali, C., Mahy, F., Rival, S., Docquier, J.D., Rossolini, G.M., et al. (2001). CENTA as a chromogenic substrate for studying β-lactamases. ANTIMICROBIAL AGENTS AND CHEMOTHERAPY, 45(6), 1868-1871 [10.1128/AAC.45.6.1868-1871.2001].
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11365/1008924
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