Purification and properties of the Mycobacterium smegmatis mc(2)155 beta-lactamase.
作者信息
Quinting B, Galleni M, Timm J, Gicquel B, Amicosante G, Frère J M
机构信息
Centre d'Ingénierie des Proteines, Université de Liège, Belgium.
出版信息
FEMS Microbiol Lett. 1997 Apr 1;149(1):11-5. doi: 10.1016/s0378-1097(97)00041-4.
PMID:9103972
Abstract
The beta-lactamase of Mycobacterium smegmatis mc(2)155 has been purified to protein homogeneity. Its N-terminal sequence and catalytic properties are similar to those of the beta-lactamase produced by Mycobacterium fortuitum D316 and establish this new enzyme as a member of molecular class A.
摘要
Zotero 插件