CENTA as a chromogenic substrate for studying beta-lactamases

Autor: Bebrone, C., Moali, C., Mahy, F., Rival, S., Docquier, Jd, Rossolini, Gm, Fastrez, J., Pratt, Rf, Frere, Jm, Galleni, M.
Přispěvatelé: Deleage, Gilbert
Jazyk: angličtina
Rok vydání: 2001
Předmět:
Popis: CENTA, a chromogenic cephalosporin, is readily hydrolyzed by beta-lactamases of all classes except for the Aeromonas hydrophila metalloenzyme. Although it cannot practically be used for the detection of beta-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.CENTA, a chromogenic cephalosporin, is readily hydrolyzed by beta-lactamases of all classes except for the Aeromonas hydrophila metalloenzyme. Although it cannot practically be used for the detection of beta-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.
Databáze: OpenAIRE