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Partial characterization of a 29 kDa cysteine protease purified from Taenia solium metacestodes
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) b...
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Main Authors: | , , , |
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Formato: | Artigo |
Idioma: | Inglês |
Publicado em: |
The Korean Society for Parasitology
2005
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Assuntos: | |
Acesso em linha: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2712020/ https://ncbi.nlm.nih.gov/pubmed/16340305 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.3347/kjp.2005.43.4.157 |
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