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Partial characterization of a 17 kDa protein of Clonorchis sinensis
A 17 kDa protein from Clonorchis sinensis adults was purified by a procedure including Sephacryl S-200 HR gel filtration and Q-Sepharose anion exchange chromatography. The protein was proved to be a cysteine protease as it showed hydrolytic activity toward Cbz-Phe-Arg-AMC in the presence of dithioth...
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| Main Authors: | , , , , |
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| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
The Korean Society for Parasitology
2000
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| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2721119/ https://ncbi.nlm.nih.gov/pubmed/10905071 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.3347/kjp.2000.38.2.95 |
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