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KMID : 0043320080310091129
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Archives of Pharmacal Research
2008 Volume.31 No. 9 p.1129 ~ p.1136
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Affinity-Purification of Fibrinogenase with High Proteolytic Activity from Agkistrodon halys (Chinese) Venom
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Ma Biao
Luo Yun-Bo
Xu Wen-Tao
Jia Jian-Ping
Wu Dan
Zhang Ying
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Abstract
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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 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.
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KEYWORD
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Fibrinogenase, Affinity-Purification, Agkistrodon halys (Chinese) venom, β-chains of fibrinogen, Fibrinolytic activity, Antithrombosis activity
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