Amicosante G, Perilli M, Felici A, Segatore B, Franceschini N, Basani F, Di Girolamo M, Oratore A
Department of Sciences and Biomedical Technologies, Faculty of Medicine and Surgery, University of Aquila, Italy.
Drugs Exp Clin Res. 1990;16(11):549-56.
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.
本研究考察了头孢噻肟（CTX）和去乙酰头孢噻肟对几种代表性β-内酰胺酶的动力学特征。对于所有研究的酶，去乙酰CTX比头孢噻肟对水解更稳定。然而，不动杆菌产生的一种头孢菌素酶可被CTX和去乙酰CTX逐步灭活。长时间孵育后，透析可部分恢复酶活性。最后，对选定的耐药菌株测试了这两种化合物。结论是，由于去乙酰CTX在体液中水解性差或半衰期长，它在体内可能有助于头孢噻肟发挥良好的抗菌性能。
