| Autor: |
Ma, Biao, Zhang, Ying, Wu, Dan, Jia, Jianping, Xu, Wentao, Luo, Yunbo |
| Zdroj: |
Archives of Pharmacal Research; Sep2008, Vol. 31 Issue 9, p1129-1136, 8p |
| Abstrakt: |
To purify and characterize the fibrinogenase with high proteolytic activity from Agkistrodon halys (Chinese) Venom. Monoclonal antibodies against fibrinogenase were prepared and a novel affinity chromatography equipped with a monoclonal antibody against fibrinogenase was developed and applied for the purification of fibrinogenases. The purified fibrinogenase was identified by fibrinolytic activity assay, and antithrombosis activity assay. HPLC chromatography and SDS-PAGE analysis demonstrated the uniformity and purity of the purified fibrinogenase. In comparison with a conventional A-50 chromatography method, affinity-purified fibrinogenase showed higher activity (3631 U mg−1 vs 501 U mg−1). In addition, the physiological activity of the fibrinogenase both in vitro and ex vivo showed the purified fibrinogenase can specifically degrade β-, γ-fibrinogen and has a high anti-thrombotic activity. In conclusion, the purified fibrinogenase by affinity column were shown to be homogeneous and showed a high and specific proteolytic activity against β-chains of fibrinogen molecules and antithrombosis activity. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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