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将序列超速离心结合凝胶层析分离纯化的Lp(a)进行L-Lysine-Sepharose4B亲和层析,分离出能与柱结合的Lp(a)Lys-和不能与柱结合的Lp(a)Lys-;进一步观察了功能异质性的上述两种Lp(a)对纤溶酶原与血小板结合的影响,结果表明:Lp(a)Lys+能有效地抑制纤溶酶原与血小板的结合,其IC50约为0.19mg/mL,而Lp(a)Lys-则无明显抑制作用。
The Lp (a) Lys- and Lp (a) which can not bind to the column were isolated by L-Lysine-Sepharose 4B affinity chromatography after ultracentrifugation and gel filtration. The effect of Lp (a) on plasminogen binding to platelets was further observed. The results showed that Lp (a) Lys + could effectively inhibit the binding of plasminogen to platelets, The IC50 was about 0.19mg / mL, while Lp (a) Lys- had no significant inhibitory effect.