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Isolation and some properties of an acid protease fromFasciola hepatica

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Summary

A new protease, detected in an extract ofFasciola hepatica, was isolated and partly purified. The pH optimum for the cleavage of denaturated haemoglobin by the enzyme is pH 3.0. This proteolytic activity is inhibited by diazoacetylnorleucine methyl ester, pepstatin, the pepsin inhibitor fromAscaris suum, and phenylalanine. The cathepsin D inhibitor from potatoes, EDTA, mercaptoethanol and the inorganic salts tested have no inhibitory effect. The cleavage of the B-chain of oxidized insulin by enzyme was studied and compared with the digestion of the same substrate by chicken and pig pepsin. The protease fromFasciola hepatica belongs to the carboxyl group of proteases and probably plays an important role in helminth nutrition.

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Authors and Affiliations

  1. Central Laboratory of Helminthology, Bulgarian Academy of Sciences, Geo Milev, Block III, 1113, Sofia, Bulgaria

    L. Rupova

  2. Institute of Organic Chemistry and Biochemistry, Czechoslovak Academy of Sciences, 166 10, Prague 6, Czechoslovakia

    H. Keilová

Authors
  1. L. Rupova
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  2. H. Keilová
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Rupova, L., Keilová, H. Isolation and some properties of an acid protease fromFasciola hepatica . Z. Parasitenkd. 61, 83–91 (1979). https://doi.org/10.1007/BF00927089

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  • DOI: https://doi.org/10.1007/BF00927089

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