| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 2830153 | Molecular and Biochemical Parasitology | 2007 | 5 Pages |
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 biolological function are discussed.
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Authors
Armin Merckelbach, Andreas Ruppel,