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目的:对根霉cw-1液体发酵生产的纤溶酶进行酶学性质初探,为天然溶栓药物的开发奠定理论基础。方法和结果:由SDS-PAGE测定该根霉纤溶酶为单一组分,相对分子量为32.5k Da;IEF电泳测定其等电点为8.3;该纤溶酶是一种糖蛋白,总含糖量为2.2%(w/v)。该纤溶酶可依次降解人血纤维蛋白的α、β和γ链。最适作用温度和p H分别为40oC和7.5;在p H5.8~10范围内,37℃保温24h,残余纤溶酶酶活在80%以上。结论:本实验研究的根霉纤溶酶可有效降解人血纤维蛋白,并且在人的正常体温下具有良好稳定性,显示了良好的溶栓药物特性。
OBJECTIVE: To study the enzymatic properties of fibrinolytic enzyme produced by liquid fermentation of Rhizopus cw-1, and to lay a theoretical foundation for the development of natural thrombolytic drugs. Methods and Results: The Rhizopus oryzae was determined as a single component by SDS-PAGE. The relative molecular weight was 32.5 kDa. The isoelectric point was 8.3 by IEF electrophoresis. The plasmin was a glycoprotein with total sugar The amount was 2.2% (w / v). This plasmin degrades α, β and γ chains of human fibrin in turn. The optimum temperature and p H were 40oC and 7.5 respectively. In the range of p H5.8 ~ 10, 37 ℃ incubated for 24h, the residual plasmin activity in more than 80%. Conclusion: Rhizopus and plasmin in this study can effectively degrade human fibrin and have good stability at normal human body temperature, showing good thrombolytic properties.