Fibrinolytic and Antithrombotic Protease from Spirodela polyrhiza

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概要

• 論文の詳細を見る

• A fibrinolytic protease was purified from a Chinese herb (Spirodela polyrhiza). The protease has a molecular mass of 145 kDa and 70 kDa in gel filtration and SDS-polyacrlamide gel electrophoresis (PAGE), respeclively, implying it is a dimer. Its optimum pH was 4.5-5.0. The enzyme was stable below 42℃ and after lyophilization. The enzyme activity was inhibited significantly by leupeptin and aprotinin. The protease hydrolyzed not only fibrin but also fibrinogen, cleaving A_α and B_β without affecting the γ chain of fibrinogen. It preferentially cleaved the peptide bond of Arg or Lys of synthetic substrates (P_1 position). The enzyme had an anticoagulating activity measured with activated thromboplastin time (APTT), thrombin time (TT), prothrombin time (PT) tests. It delayed APTT, TT, PT two times at the concentration of 36,39,and nM, respectively and this was drastically reduced treatment.

• 社団法人日本農芸化学会の論文
• 2001-04-23

著者

• Choi Hye-seon

  Dep. Of Biological Sciences And Immunomodulation Res. Center Univ. Of Ulsan

• CHOI Hye-Seon

  Department of Biological Sciences and Immunomodulation Research Center, University of Ulsan

• Choi Hye-seon

  Department Of Biological Sciences (bk21 Program) And Immunomodulation Research Center University Of

• SA You-Seon

  Department of Biological Sciences, University of Ulsan

• Sa You-seon

  Department Of Biological Sciences University Of Ulsan

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