摘要
Dear Editor, Enteropeptidase （enterokinase, EC 3.4.21.9） is a serine protease, which shows a specific cleavage of its substrates at the C-terminal of the recognition site （Asp）4Lys （Zheng et al., 2009）. Because of the unique specificity, enteropep- tidase could be used as a tool for the production of recom- binant fusion proteins. Especially the recombinant enteropeptidase light chain （EPL）, which contains a catalytic domain, is of large interest to be applied in biopharmaceu- tical industry （Lu et al., 1997）.
Dear Editor, Enteropeptidase （enterokinase, EC 3.4.21.9） is a serine protease, which shows a specific cleavage of its substrates at the C-terminal of the recognition site （Asp）4Lys （Zheng et al., 2009）. Because of the unique specificity, enteropep- tidase could be used as a tool for the production of recom- binant fusion proteins. Especially the recombinant enteropeptidase light chain （EPL）, which contains a catalytic domain, is of large interest to be applied in biopharmaceu- tical industry （Lu et al., 1997）.
