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Purification and properties of the Mycobacterium smegmatis mc(2)155 beta-lactamase
B Quinting1, M Galleni, J Timm
1Centre d'Ingénierie des Proteines, Université de Liège, Belgium.
FEMS Microbiology Letters
|April 1, 1997
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.