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赤子爱胜蚓五种纤溶酶组分的分离纯化及对纤维蛋白原酶解的初步研究
PURIFICATION OF FIVE FIBRINOLYTIC ENZYMES FROM THE EARTHWORM (EISENIA FOELIDE) AND STUDIES ON FIBRINOGEN ENZYMOLYSIS
【摘要】 经硫酸铵盐析沉淀和PAGE制备电泳,从赤子爱胜蚓(Eiseniafoelide)粗品中分离纯化出五种纤溶酶组份(Ⅰ、Ⅶ、Ⅷ、Ⅸ、Ⅹ),在PAGE中均呈现单一带。组份Ⅶ、Ⅷ、Ⅹ能将纤维蛋白原中α、β、γ链依次降解,对α链亲和力最大。组份X不能降解43.5KD、40KD、24.5KD片段。组份Ⅰ对α链有较高亲和力而对γ链无降解作用。
【Abstract】 By ammonium sulfate precipitation and preparative electrophoresis, five fibrinolytic enzymes(Ⅰ、Ⅶ、Ⅷ、Ⅸ、Ⅹ) were isolated and purified from the extract of the earthworm (Eisenia foelide), they were single band determined by PAGE. The α,β,γ chains of fibrinogen were successively degraded by EFE Ⅶ,Ⅷ,Ⅸ and Ⅹ respectively, and had the most affinity to α chain. Component X can not degrade the fragment of 43.5,40,24 5 KD. Component I had high affinity to α chain, but can not degrade r chain.
- 【文献出处】 华西药学杂志 ,WEST CHINA JOURNAL OF PHARMACEUTCAL SCIENCES , 编辑部邮箱 ,1999年01期
- 【分类号】TQ464.8
- 【被引频次】42
- 【下载频次】176