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자료유형
학술저널
저자정보
Ma, Biao (College of Food Science & Nutritional Engineering, China Agricultural University) Zhan, Ying (Saisheng Pharmaceutical Company) Wu, Dan (Saisheng Pharmaceutical Company) Jia, Jianping (Department of Neurology XuanWU Hospital, Capital University of Medical Sciences) Xu, Wentao (College of Food Science & Nutritional Engineering, China Agricultural University) Luo, Yunbo (College of Food Science & Nutritional Engineering, China Agricultural University)
저널정보
대한약학회 Archives of pharmacal research : a publication of the Pharmaceutical Society of Korea Archives of pharmacal research : a publication of the Pharmaceutical Society of Korea 제31권 제9호
발행연도
2008.1
수록면
1,129 - 1,136 (8page)

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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 $\beta$-, $\gamma$-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 $\beta$-chains of fibrinogen molecules and antithrombosis activity.

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