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題 名 | Purification and Characterization of a Novel Fibrinolytic Protease from Schizophyllum Commune=裂褶菌(Schizophyllum commune)溶纖活性蛋白分離純化與其特性分析 |
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作 者 | 呂仲倫; 陳士鈞; 陳秀男; | 書刊名 | Journal of Food and Drug Analysis |
卷 期 | 18:2 2010.04[民99.04] |
頁 次 | 頁69-76+137 |
分類號 | 435.29 |
關鍵詞 | 裂褶菌; 菇蕈類; 模掃式過濾; 溶纖活性蛋白; 抗血栓活性; Schizophyllum commune; Mushroom; Cross-flow filtration; Fibrinolytic protease; Antithrombotic; |
語 文 | 英文(English) |
英文摘要 | ABSTRACT Schizophyllum commune, a widely distributed medicinal mushroom, was found with fibrinolytic activity from its basidiomycetes. The fibrinolytic activity of S. commune was to be beneficial for antithrombotic therapy. In this study, S. commune was cultured with fermentation technology, and protease purification was carried out by cross-flow filtration and fast performance liquid chromatography (FPLC) system. The specific activity of S. commune fibrinolytic protease increased 9.29-fold over the culture broth after purification. The fibrinolytic protease shows superior fibrinolytic activity than human plasmin and is inhibited by EDTA. Characterizations of this protease showed 21.32 kDa in molecular mass and monomeric form in protein structure. The optimal protease activity reveals at pH 5.0 and 45°C, and is enhanced by magnesium. |
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