【摘要】 通过选择性热变性、大豆胰蛋白酶抑制剂 - Sepharose4B亲和层析、DEAE-纤维素离子交换层析和 Arg- Sepharose 4B亲和层析 ,从双胸蚓中分离纯化得到具有强烈纤溶活性的酶组分。经 PAGE检定为单一谱带 ,分子量约为 32 k D,等电点约 3.3。该酶组分具有热稳定性 ,p H稳定性和宽的最适 p H范围 ,能被 TI及 PMSF抑制 ,不被 PCMB抑制 ,属丝氨酸蛋白酶更多还原

【Abstract】 A strong fibrinolytic enzyme was purified from earthworm Lumbircidae Bimastos The procedure of purification included heat selective denaturation, TI(Trypsin Inhibitor) Sepharose 4B affinity chromatography,DEAE cellulose ion exchange chromatography and L Arg Sepharose 4B affinity chromatography The purified component was proved to be homogenous in PAGE electrophoresis The molecular weight and isoelectric point were about 32000 and 3 3, respectively The enzyme was heat stable,pH stable and displayed a broad optimal pH range TI and PMSF strongly inhibited the enzyme,but PCMB exerted little effect under the same conditions, which represented a serine protease更多还原