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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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Autors principals: Kim, Ji-Young, Yang, Hyun-Jong, Kim, Kwang-Sig, Chung, Young-Bae
Format: Artigo
Idioma:Inglês
Publicat: The Korean Society for Parasitology 2005
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Accés en línia: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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