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目的:从蛇毒中获得大量高纯度的具有激肽原酶活性的蛋白水解酶。方法:采用离子交换和亲和层析技术进行纯化。结果:从江浙蝮蛇毒中提取出了一种高纯度的具有激肽原酶活性的蛋白水解酶,不需活化即可水解激肽原,释放激肽,并具有精氨酸酯酶活性。粗毒经提纯,比活可达800U/mg以上,远远高于哺乳动物来源的激肽原酶,纯度可达95%以上。对其性质考察,Mr为38000,N-末端的15个氨基酸序列分析表明,该酶与蛇毒丝氨酸蛋白酶及胰蛋白酶——激肽释放酶同源。结论:这种方法适合于工业化生产。
Objective: To obtain a large number of high-purity proteolytic enzymes with kininogenase activity from snake venoms. Methods: Purification was performed using ion exchange and affinity chromatography techniques. RESULTS: A high-purity proteolytic enzyme with kininogenase activity was extracted from Jiangsu and Zhejiang venom venoms. It can hydrolyze kininogen without activation, release kinins, and possess arginine esterase activity. Crude virus after purification, specific activity up to 800U/mg or more, far higher than the mammalian source of kininogenase, the purity of up to 95%. For its properties, Mr was 38000. The N-terminal 15 amino acid sequence analysis showed that the enzyme is homologous to snake venom serine protease and trypsin kallikrein. Conclusion: This method is suitable for industrial production.