采用离子交换层析、凝胶过滤层析及快速蛋白液相色谱等蛋白质分离纯化技术,从白黄侧耳菌丝体中纯化一种溶栓酶,并进行酶学性质研究。实验结果表明,其分子质量约为18 ku,该酶的最适pH和最适温度为pH 7.0,40℃,并对糜蛋白酶底物S-2586最敏感。Co2+和Mg2+激活该酶活性,而Cu2+、EDTA对酶活有抑制作用。该酶不仅可直接水解纤维蛋白,还可以水解纤维蛋白原。

A Fibrinolytic enzyme was purified from the mycelia of Pleurotus cornucopiae by ion exchange chromatography followed by gel filtration and fast protein liquid chromatography.Study the factors affected on the fibrinolytic activity of fibrinolytic enzyme from the mycelia of Pleurotus cornucopiae,and examine the fibrinolytic specialty on fibrin and fibrinogen and amidolytic activity.The apparent molecular mass of purified enzyme was estimated to be 18 ku.Its optimal pH and temperature value were 7.0 and 40℃,respectively,and it was found to exhibit a higher specificity for the substrate S-2586 for chymotrypsin.Enzyme activity was enhanced by Co2+ and Mg2+,but inhibited by the addition of Cu2+ and EDTA.The mycelia of Pleurotus cornucopiae may thus represent a potential source of new therapeutic agents to treat thrombosis.