摘要
蚯蚓纤溶酶（ＥＰＡ）抽提液经３０％ ～７０％ 饱和度的（ＮＨ４）２ＳＯ４ 盐析、ＤＥＡＥ—纤维素柱层析、Ｓｅｐｈａｄｅｘ Ｇ－７５葡聚糖凝胶过滤等纯化步骤，得到了具有纤溶活性的洗脱峰，置凝胶电泳后，得到四个活性组分，它们经５０℃保温６ｈ，活力上升６４％ ；在２ ｍ ｏｌ／Ｌ盐酸胍存在时，活力仅保存７．２％ ，当其浓度降低时，活力可恢复至９０％ ；在１％ ＳＤＳ存在时，活力仅保存１２．１％ ，但当ＳＤＳ除去时，活力又可恢复。因此，盐酸胍、ＳＤＳ均为ＥＰＡ 可逆性抑制剂。另外，ＥＰＡ 中含有较高的糖链（占总量的４５％ ），具有良好的抵抗自水解作用。
The fibrinolytic enzyme, earthworm plasminogen activitor (EPA) or lumbrokinase (LK), was extracted and purified form the earthworm, Eisenia foelide , by a procedure of 30～70%(NH 4) 2SO 4 precipitation, DEAE cellulose exchange chromatograph and Sephadex G 75 gel filtration. And some properties of the enzyme have been studied. EPA’s optimal reaction temperature is 50° C. And after incubating at 50° C for 6 hours, its activity was increased 64%. When the enzyme was incubated in 2mol/L GuHCl and 1% SDS, the activity was decreased to 7.2% and 12.1% respectively, and as the concentration of denaturants decreased, the activity came up again. It seems that the high content of glycosyl residues contributes to the enzyme resistance to hydrolysis.
出处
《氨基酸和生物资源》
CAS
1999年第4期34-38,共5页
Amino Acids & Biotic Resources
