國?臺灣大學漁業科學研究所; 國?臺灣大學生命科學院 生命科學系Institute of Fisheries Science, National Taiwan University; Department of Life Science, College of Life Science, National Taiwan University?仲?陳秀男Lu, C.L.C.L.LuChen, S.N.S.N.Chen2017-09-122018-07-062017-09-122018-07-062010-06http://ntur.lib.ntu.edu.tw//handle/246246/283362近??，已發展國家中的人們對於預防以及治?血栓性疾病，皆投注以相當高的關注，而同時，科學家們也希望由研究中，可再找到?經濟與安全性?高的抗血栓藥物，?治?血栓性疾病。由本實驗室先前的研究發現，自菇蕈?-?褶菌 (Schizophyllum commune)醱酵培養物中，有一個具備溶解纖維蛋白活性的活性蛋白? (fibrinolytic protease)；於本篇研究中，此溶纖蛋白?再被證明其具有效溶解血液凝塊的作用；並且，由實驗篩選出對此溶纖蛋白?活性，具有?激效果的二價?屬?子，進一步使用溶纖蛋白?與二價?屬?子共同之處?，觀察其對大鼠血液血栓彈?圖譜 (thromboelastography, TEG)之影響，研究血液凝固作用的進?，與當中各項??變化。由結果發現，鎂?子具有最明顯提升溶纖蛋白?活性，且於大鼠血液血栓彈?圖譜分析，鎂?子與溶纖蛋白?的添加亦顯著地?低血液凝固強? (clotting strength)，而無抑制血液凝固發生與進?速?之影響。因此，總結以上結果，鎂?子提升作用具有提高溶纖蛋白?抗血栓形成的有?影響性；而此，本篇文章為首?以血液血栓彈?圖譜分析，觀察真菌溶纖蛋白?對抗血栓形成影響的研究，並且也指出鎂?子對於提昇?褶菌溶纖蛋白?抗血栓活性的有效性。Prevention and therapy of thrombotic diseases have attracted much attention in developed countries during recent years. Investigators have been looking for cheaper and safer thrombolytic agents for therapy of thrombotic diseases. Recently, we have discovered a fibrinolytic protease from Schizophyllum commune. In this study, the protease was proven to degrade blood clot effectively. Seven divalent metal ions were used to test the selectiveness on enhancing protease activity. The treated rat blood was traced by thromboelastography to assess the viscoelastic properties of whole blood. As the result, fibrinolytic activity of the protease was enhanced remarkably by Mg2+ in reducing the strength of blood clot and showed the innovative anti-thrombotic effects. This is the first study of anti-thrombotic effects from fungal-derived fibrinolytic protease using thromboelastography and delineates the efficacy of magnesium supplementation in enhancement of thrombolytic activity from S. commune fibrinolytic protease.4792794 bytesapplication/pdfFibrinolytic proteaseSchizophyllum communeMagnesiumAnti-thromboticThromboelastography溶纖蛋白??褶菌鎂?子抗血栓形成血液血栓彈?圖。journal articlehttp://ntur.lib.ntu.edu.tw/bitstream/246246/283362/1/5502_201006_4.pdf