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三氟沙星的体外活性及其对肺炎链球菌青霉素结合蛋白的亲和力。

In vitro activity of sanfetrinem and affinity for the penicillin-binding proteins of Streptococcus pneumoniae.

作者信息

Sifaoui F, Varon E, Kitzis M D, Gutmann L

机构信息

L.R.M.A., Université Paris VI, France.

出版信息

Antimicrob Agents Chemother. 1998 Jan;42(1):173-5. doi: 10.1128/AAC.42.1.173.

Abstract

Against penicillin-susceptible pneumococci, the activity of sanfetrinem was similar to those of penicillin, amoxicillin, cefotaxime, imipenem, and meropenem, while against penicillin-resistant strains, sanfetrinem and the carbapenems exhibited superior activity (MICs at which 90% of strains are inhibited, < or =1 microg/ml). PBP 1a in the penicillin-susceptible strain and PBP 1a and PBP 2b in the more resistant isolates seemed to be the essential penicillin-binding proteins for imipenem and sanfetrinem.

摘要

针对对青霉素敏感的肺炎球菌,三唑巴坦的活性与青霉素、阿莫西林、头孢噻肟、亚胺培南和美罗培南相似,而针对耐青霉素菌株,三唑巴坦和碳青霉烯类药物表现出更强的活性(90%菌株被抑制时的最低抑菌浓度,≤1微克/毫升)。对青霉素敏感菌株中的青霉素结合蛋白1a以及耐药性更强的菌株中的青霉素结合蛋白1a和青霉素结合蛋白2b似乎是亚胺培南和三唑巴坦的关键青霉素结合蛋白。

相似文献

7
Penicillin-binding proteins of Streptococcus pneumoniae.肺炎链球菌的青霉素结合蛋白
J Antimicrob Chemother. 1988 Dec;22(6):791-800. doi: 10.1093/jac/22.6.791.

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