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蚯蚓纤溶酶新组分的分离纯化及部分性质 被引量:3

Purifi cation and Partial Properties of New Components of Earthworm Fibrinolytic Enzymes
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摘要 采用以大豆胰蛋白酶抑制剂为配基的亲和色谱分离蚯蚓纤溶酶,以DEAE-纤维素-52离子交换柱色谱和制备电泳纯化各单组分。结果表明新组分8、9、10都是能水解纤维蛋白的糖蛋白。组分8是一种纤溶酶原激活剂,有2个亚基,Mr为25.5k和17.8k;组分9仅一条肽链,Mr为33.6k;组分10含有Mr为18.7k和10.9k的2个亚基。组分9、10均兼有纤溶酶原激活活性和直接纤溶活性。 Earthworm fibrinolytic enzyme components were separated by affinity chromatography with soybean trypsin inhibitor as ligand. Single components were purified through DEAE-cellulose-52 chromatography and preparative electrophoresis. New components 8, 9 and 10 are all glycoproteins capable of hydrolyzing fibrin. Component 8 is a plasminogen activator consisting of two subunits of 25.5k and 17.8k. Component 9 is only one polypeptide of 33.6k, and component 10 contains two subunits of 18.7k and 10.9k. Both component 9 and 10 showed plasminogen-activating and fibrinolytic activities.
出处 《中国医药工业杂志》 CAS CSCD 北大核心 2008年第6期420-422,共3页 Chinese Journal of Pharmaceuticals
基金 河北省自然科学基金项目(C2005000118)
关键词 蚯蚓纤溶酶 纤溶酶原激活剂 糖蛋白 分离纯化 earthworm fibrinolytic enzyme plasminogen activator glycoprotein separation and purification
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参考文献12

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