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  • Title: Purification of a cathepsin L-like proteinase secreted by adult Fasciola hepatica.
    Author: Smith AM, Dowd AJ, McGonigle S, Keegan PS, Brennan G, Trudgett A, Dalton JP.
    Journal: Mol Biochem Parasitol; 1993 Nov; 62(1):1-8. PubMed ID: 8114809.
    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.
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