Purification of a cathepsin L-like proteinase secreted by adult Fasciola hepatica

A M Smith, A J Dowd, S McGonigle, P S Keegan, G Brennan, A Trudgett, J P Dalton

Research output: Contribution to journalArticle

136 Citations (Scopus)

Abstract

A cysteine proteinase released in vitro by Fasciola hepatica was purified to homogeneity by Sephacryl S-200 gel filtration chromatography followed by QAE-Sephadex chromatography. The purified enzyme resolves as a single band with an apparent molecular size of 27 kDa on reducing SDS-polyacrylamide gel electrophoresis; however, under non-reducing conditions it migrates as multiple bands, each with enzymatic activity, in the apparent molecular size range 60-90 kDa. The sequence of the first 20 N-terminal amino acids of the enzyme shows considerable homology with cathepsin L-like proteinases. Immunolocalisation studies revealed that the cathepsin L-like proteinase is concentrated within vesicles in the gut epithelial cells of liver fluke.
Original languageEnglish
Pages (from-to)1-8
Number of pages8
JournalMolecular and Biochemical Parasitology
Volume62
Issue number1
Publication statusPublished - Nov 1993

Keywords

  • Amino Acid Sequence
  • Animals
  • Cathepsin L
  • Cathepsins
  • Cattle
  • Chromatography, Gel
  • Chromatography, Ion Exchange
  • Cysteine Endopeptidases
  • Endopeptidases
  • Enzyme Precursors
  • Fasciola hepatica
  • Humans
  • Immunoblotting
  • Immunohistochemistry
  • Molecular Sequence Data
  • Rats
  • Sequence Homology, Amino Acid
  • Species Specificity

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