In this study the kinetic features of cefotaxime (CTX) and desacetyl-cefotaxime towards several representative β-lactamases were investigated. Desacetyl-CTX was more stable to hydrolysis in comparison with cefotaxime for all the investigated enzymes. However, a cephalosporinase produced in Acinetobacter was progressively inactivated by both CTX and des-CTX. After prolonged incubation, dialysis partially restored the enzyme activity. Finally, both compounds were tested against selected resistant strains. It is concluded that des-CTX, because of either poor hydrolysis or prolonged half-life in body fluids, could contribute in vivo to the good antimicrobial properties of cefotaxime.
CTX and its desacetyl derivative (des-CTX): Interaction with some representative β-lactamases and their related pattern of resistance to newer selected clinical isolates
AMICOSANTE, Gianfranco;PERILLI, MARIAGRAZIA;SEGATORE, Bernardetta;FRANCESCHINI, Nicola;ORATORE, Arduino
1990-01-01
Abstract
In this study the kinetic features of cefotaxime (CTX) and desacetyl-cefotaxime towards several representative β-lactamases were investigated. Desacetyl-CTX was more stable to hydrolysis in comparison with cefotaxime for all the investigated enzymes. However, a cephalosporinase produced in Acinetobacter was progressively inactivated by both CTX and des-CTX. After prolonged incubation, dialysis partially restored the enzyme activity. Finally, both compounds were tested against selected resistant strains. It is concluded that des-CTX, because of either poor hydrolysis or prolonged half-life in body fluids, could contribute in vivo to the good antimicrobial properties of cefotaxime.Pubblicazioni consigliate
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