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.
|Titolo:||CTX and its desacetyl derivative (des-CTX): Interaction with some representative β-lactamases and their related pattern of resistance to newer selected clinical isolates|
|Autori interni:||AMICOSANTE, Gianfranco|
|Data di pubblicazione:||1990|
|Rivista:||DRUGS UNDER EXPERIMENTAL AND CLINICAL RESEARCH|
|Appare nelle tipologie:||1.1 Articolo in rivista|