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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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

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.[1]

References

  1. Purification of a cathepsin L-like proteinase secreted by adult Fasciola hepatica. Smith, A.M., Dowd, A.J., McGonigle, S., Keegan, P.S., Brennan, G., Trudgett, A., Dalton, J.P. Mol. Biochem. Parasitol. (1993) [Pubmed]
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