Short communication: Biochemical properties of an intracellular serpin from Echinococcus multilocularis

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...

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Published inMolecular and biochemical parasitology Vol. 156; no. 1; pp. 84 - 88
Main Authors Merckelbach, Armin, Ruppel, Andreas
Format Journal Article
LanguageEnglish
Published 01.11.2007
Subjects
Echinococcus multilocularis
Escherichia coli
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Summary: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.
Bibliography:ObjectType-Article-1
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ISSN:0166-6851
DOI:10.1016/j.molbiopara.2007.07.013