摘要
以肝素琼脂糖亲和层析和超速离心分离了盐源山蛭(Haemendipsayanyuanensis)的抗凝血蛋白,抗凝血活性试验证明,该蛋白不抑制凝血因子Xa的活性,而显著抑制凝血酶的活性.亲和层析的蛋白洗脱峰与抗凝血酶的活力峰相吻合,因此,盐源山蛭抗凝血蛋白属于凝血酶特异性的抗凝血蛋白.
An anticoagulant protein is isolated from Yanyuan led (Haemendipsa yanyuanensiS) by heparin agarose affinity chromatography and ultracentrifugation. Using the method of chromogenic substrate, the anticoagulant activity of the protein is measured, the results indicate that the inhibitor is thrombin-specific but not factor Xa-specific. The elution peaks at UV 280nm of the protein in the affinity chromatograph are in correspondence with the antithrombin activity peaks at 405nm. So that the anticoagulant protein isolated from yanyuan leech is thrombin-specific anticoagulant protein can be concluded.
出处
《北京师范大学学报(自然科学版)》
CAS
CSCD
北大核心
1998年第1期115-118,共4页
Journal of Beijing Normal University(Natural Science)
基金
美国日立化学研究中心资助
关键词
盐源山蛭
抗凝血蛋白
凝血酶
凝血因子XA
Haemendipsa yanyuanensis, anticoagulant protein
thrombin
factor Xa