| Literature DB >> 17727977 |
Armin Merckelbach1, Andreas Ruppel.
Abstract
A serpin of the intracellular type from the tapeworm Echinococcus multilocularis was expressed in Escherichia coli, purified by ion exchange chromatography and tested for inhibitory activity against several proteinases. The recombinant protein, which after transcriptional induction, represents about 20 % of total cellular protein, is biochemically active and inhibits trypsin and the trypsin-like plasmin as well as pig pancreatic and human neutrophil elastase. Implications regarding its biochemistry and biological function are discussed.Entities:
Mesh:
Substances:
Year: 2007 PMID: 17727977 DOI: 10.1016/j.molbiopara.2007.07.013
Source DB: PubMed Journal: Mol Biochem Parasitol ISSN: 0166-6851 Impact factor: 1.759