摘要
芽孢杆菌 2 # (Bs- 2 )的发酵液经过硫酸铵分级沉淀、SephadexG - 75凝胶过滤层析、Q -Sepharose阴离子交换层析、电泳制备和电洗脱 ,获得一种具有纤溶活性的蛋白酶 ;该蛋白酶由 3个亚基组成 ,分子量分别约为 2 3KD ,2 2KD ,19KD ,全酶分子量约为 6 4KD ;经纤维蛋白平板测定表明 ,该酶既具有纤溶酶作用 。
A fibrinolytic enzyme was purified from the crude extract of Bs-2,a strain of Bacillus sp .,through ammonium sulphate fractional precipitation,Sephadex G-75 gel filtration,Q-Sepharose anion exchange chromatography,preparative PAGE and electric elution.The purified component was shown to consist of three subunits with a molecular weight of approximately 23,22 and 19 kD,respectively,and the molecular weight of the enzyme was about 64 kD.The enzyme showed similar fibrinolytic activity on the fibrin plate and the plasminogen-free fibrin plate,suggesting that it may contain both strong thrombolytic enzyme activity and plasminogen activator activity.
出处
《西南农业大学学报（自然科学版）》
CSCD
北大核心
2001年第1期66-69,共4页
Journal of Southwest Agricultural University
关键词
芽孢杆菌
纤溶酶
纯化
生物活性
Bacillus sp .
fibrinolytic enzyme
purification
bioactivity
