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Parasitology Research

, Volume 86, Issue 8, pp 684–687 | Cite as

Partial characterization of serine proteinases secreted by adult Trichinella spiralis

  • Valentina K. Todorova
  • Dimitar I. Stoyanov
ORIGINAL PAPER

Abstract

Serine proteinases secreted by adult Trichinella spiralis were isolated from excretory/secretory products (ES) of in-vitro-cultured parasites by affinity chromatography with p-benzamidine-celite. The purified enzymes had molecular weights of approximately 18, 40, and 50 kDa and displayed enzyme activity against a range of low-molecular-weight substrates, gelatin, and azocasein. The antigenicity of these parasite proteinases was demonstrated by the inhibition of enzymatic activity with IgG purified from infected hosts. The inactivation of major secreted proteinases of adult T. spiralis by immune antibody could presumably contribute to impairment of the survival of the parasite in sensitized hosts.

Keywords

Molecular Weight Enzymatic Activity Serine Gelatin Serine Proteinase 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer-Verlag Berlin Heidelberg 2000

Authors and Affiliations

  • Valentina K. Todorova
    • 1
  • Dimitar I. Stoyanov
    • 1
  1. 1.Institute of Molecular Biology, Bulgarian Academy of Sciences, Academik G. Bonchev Street, Building 21, 1113 Sofia, Bulgaria e-mail: vtodorov@obzor.bio21.bas.bg Tel.:/Fax: +3592-736450BG

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