Adsorption and inactivation of proteolytic enzymes by Triaenophorus nodulosus (Cestoda)

G.I. Izvekova 1 , T.V. Frolova 1  and E.I. Izvekov 1
  • 1 I.D. Papanin Institute for Biology of Inland Waters, Russian Academy of Sciences, Borok, Nekouzskii raion, Yaroslavskaya oblast, 152742, Russian Federation

Summary

The proteolytic activity in washings off the Triaenophorus nodulosus cestode tegument and the ability of the worms to inactivate proteolytic enzymes were studied. It was found that the major proteolytic activity in the washing samples is represented by the easily desorbed fraction most probably characterizing the activity of the host’s enzymes. Serine proteinases are an essential part of these enzymes. It was shown that the worms’ incubation medium and their homogenates can inhibit host proteinases and commercial trypsin samples. Suppressive activity of the incubation medium suggests that the inhibitors are rather spontaneously produced by the worms than induced by the presence of proteinases in the surrounding medium. The inhibitor produced by the cestode is hypothesized to be trypsin-specific.

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HELMINTHOLOGIA is a scientific journal of the Slovak Academy of Sciences published quarterly in English by Institute of Parasitology SAS, Slovak Republic. The journal is a medium for publication of original previously unpublished scientific papers from different fields of helminthology. The role of the journal is to enrich the theoretical basis of helminthology and to contribute to the advancement in human and veterinary medicine and agronomy.

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