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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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| Asıl Yazarlar: | , , , , |
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| Materyal Türü: | Artigo |
| Dil: | Inglês |
| Baskı/Yayın Bilgisi: |
The Korean Society for Parasitology
2000
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| Konular: | |
| Online Erişim: | 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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