痢疾志贺氏菌SHV-11β-内酰胺酶的分子特征
Molecular characterization of the SHV-11 beta-lactamase of Shigella dysenteriae.
作者信息
Ahamed J, Kundu M
机构信息
Department of Chemistry, Bose Institute, Calcutta 700 009, India.
出版信息
Antimicrob Agents Chemother. 1999 Aug;43(8):2081-3. doi: 10.1128/AAC.43.8.2081.
Abstract
A beta-lactamase with an M(r) of 29,000 and a pI of 7.6 was partially purified from a clinical isolate of Shigella dysenteriae. The bla gene encoded the SHV-11 enzyme carrying the substitution Leu-->Gln at position 35 and was linked to a strong promoter. This variant, unlike the prototype SHV-1 enzyme, hydrolyzed oxacillin, cloxacillin, and oxyiminocephalosporins such as cefotaxime.
摘要
从痢疾志贺氏菌的临床分离株中部分纯化出一种分子量为29,000、等电点为7.6的β-内酰胺酶。bla基因编码携带第35位Leu→Gln替换的SHV-11酶，并与一个强启动子相连。与原型SHV-1酶不同，这种变体可水解苯唑西林、氯唑西林和氧亚氨基头孢菌素如头孢噻肟。
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