Objective: To separate and purify a novel thrombolytic enzyme (FSC2-13) from culture media of an induced Bacillus subtilis strain and to study its in vitro and in vivo thrombolytic activities.

Methods: Employed fibrin plate method, pyrogenation (heating up) fibrin plate method and SDS-PAGE were used respectively to study FSC2-13 hydrolyzing fibrin and fibrinogen in vitro. Investigations were made on its in vivo pharmacodynamics using rat thrombogenesis inhibition model after it was administrated by intestinal route.

Results: FSC2-13 could hydrolyze fibrin and fibrinogen in vitro and had hydrolysis sites on three peptide chains of fibrinogen. FSC2-13 could significantly inhibit the formation of rat venous thrombus after being administrated by intestinal route. Thrombogenesis inhibition rate was 68%. Activated partial thromboplastin time increased by 51%, fibrinogen content decreased by 49%, fibrin degradation product (FDP) content also increased obviously, but the plasminogen content did not change obviously.

Conclusion: FSC2-13 possessed in vitro and in vivo thrombolytic activities in a special way. There seem to be prospects for researches to develop it into a new generation of oral thrombolytic drug.

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