Biochemical properties of an intracellular serpin from Echinococcus multilocularis

Mol Biochem Parasitol. 2007 Nov;156(1):84-8. doi: 10.1016/j.molbiopara.2007.07.013. Epub 2007 Jul 24.

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.

MeSH terms

  • Animals
  • Echinococcus multilocularis / enzymology*
  • Echinococcus multilocularis / genetics
  • Escherichia coli / enzymology
  • Escherichia coli / genetics
  • Helminth Proteins / chemistry
  • Helminth Proteins / genetics
  • Helminth Proteins / isolation & purification
  • Helminth Proteins / metabolism
  • Humans
  • Leukocyte Elastase / antagonists & inhibitors
  • Pancreatic Elastase / antagonists & inhibitors
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • Serpins* / chemistry
  • Serpins* / genetics
  • Serpins* / isolation & purification
  • Serpins* / metabolism
  • Trypsin Inhibitors / metabolism

Substances

  • Helminth Proteins
  • Recombinant Proteins
  • Serpins
  • Trypsin Inhibitors
  • Pancreatic Elastase
  • Leukocyte Elastase