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经过 75 %饱和度硫酸铵沉淀、SephadexG 75凝胶过滤层析、Lys Sepharose 4B亲和层析和电泳制备洗脱 ,从华广虻 (TabanusamaenusWalker)腹部组织匀浆液中分离纯化出分子量约为 6 7KD的溶纤活性蛋白TAFP。经纤维蛋白平板测定表明 ,TAFP不仅具有纤溶酶作用 ,还具有激活纤溶酶原的作用 ;通过三肽生色底物测定发现 ,TAFP能分解纤溶酶原激活剂的生色底物—ChromozymUK及S 2 2 88。还能水解胰蛋白酶专一底物Bz Phe Val Arg NA及CBZ Gly Pro Arg NA ,表明TAFP具有类胰蛋白酶活性 ,专一水解精氨酸形成的酰胺键 (或肽键 )。TAFP无胰凝乳蛋白酶活性
After 75% saturation ammonium sulfate precipitation, Sephadex G 75 gel filtration chromatography, Lys Sepharose 4B affinity chromatography and electrophoresis preparative elution, from the abdominal tissue homogenate of Tabanus australasia (Tabanusamaenus Walker) purified molecular weight of about 67KD Of fibrinolytic active protein TAFP. The fibrin plate assay showed that TAFP not only has the role of plasmin but also activates plasminogen; by tripeptide chromogenic substrate assay, TAFP can break down the chromogenic substrate of plasminogen activator - ChromozymUK and S 2 2 88. It also hydrolyzes the trypsin-specific substrates Bz Phe Val Arg NA and CBZ Gly Pro Arg NA, indicating that TAFP has tryptase activity and specifically hydrolyzes amide bonds (or peptide bonds) formed by arginine. TAFP has no chymotrypsin activity