ArticleThe Korean journal of parasitology2005
Partial characterization of a 29 kDa cysteine protease purified from Taenia solium metacestodes.
Article in The Korean journal of parasitology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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2 citing papers in PubMed, 9 citations in OpenAlex.
- Molecular characterization of EcCLP1, a new putative cathepsin L protease from Echinococcus canadensis.Parasite (Paris, France) · 2024Article
- Partial purification and characterization of a cysteine protease inhibitor from the plerocercoid of Spirometra erinacei.The Korean journal of parasitology · 2008Article
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4 authors at 1 institution in 1 country.
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Abstract
A 29 kDa cysteine protease of Taenia solium metacestodes was purified by Mono Q anion-exchanger and Superose 6 HR gel filtration chromatography. The enzyme was effectively inhibited by cysteine protease inhibitors, such as iodoacetic acid (IAA) and trans-epoxy-succinyl-L-leucyl-amido (4-guanidino) butane (E-64) while inhibitors acting on serine- or metallo-proteases did not affect the enzyme activity. The purified enzyme degraded human immunoglobulin G (IgG), collagen and bovine serum albumin (BSA), but human IgG was more susceptible for proteolysis by the enzyme. To define the precise biological roles of the enzyme, more detailed biochemical and functional studies would be required.
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