CTX and its desacetyl derivative (des-CTX): interaction with some representative beta-lactamases and their related pattern of resistance to newer selected clinical isolates.
In this study the kinetic features of cefotaxime (CTX) and desacetyl-cefotaxime towards several representative beta-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.
Amicosante
G
G
Department of Sciences and Biomedical Technologies, Faculty of Medicine and Surgery, University of Aquila, Italy.
Perilli
M
M
Felici
A
A
Segatore
B
B
Franceschini
N
N
Basani
F
F
Di Girolamo
M
M
Oratore
A
A
D000900:Anti-Bacterial Agents / Q000494:pharmacology; D002439:Cefotaxime / Q000031:analogs & derivatives* / Q000494:pharmacology*; D004352:Drug Resistance, Microbial; D004755:Enterobacteriaceae / Q000187:drug effects; D007700:Kinetics; D008826:Microbial Sensitivity Tests; D065093:beta-Lactamase Inhibitors
D000900:Anti-Bacterial Agents; D065093:beta-Lactamase Inhibitors; C029281:desacetylcefotaxime; D002439:Cefotaxime