蚌蛙蛭抗凝血蛋自的分离及抗凝血特性(英文)

ISOLATION AND CHARACTERIZATION OF AN ANTICOAGULANT PROTEIN FROM THE LEECH BATRACOBDELLA KASMIANA

以超速离心和肝素琼脂糖亲和层析从蚌蛙蛭（Batracobdellakasmiana）的粗提取液中分离到2种抗凝血蛋白．抗凝血活性测定证明，这2种蛋白具有显著抑制凝血酶的活性而不具有抑制凝血因子Xa的活性．亲和层析的蛋白洗脱峰与抑制凝血酶的活力峰相吻合；因此，蚌蛙蛭的抗凝血蛋白是属于凝血酶特异性的抗凝血蛋白．这为进一步研究蚌蛙蛭抗凝血蛋白的抗凝血机理及其应用打下了基础．

Two components of anticoagulant protein are isolated from the leech Batracobdella kasmiana by heparin agarose affinity chromatography and ultracentrifugation. The determination of anticoagulant activity and characterization analysis of the protein using the method of chromogenic substrate indicate that the anticoagulant protein is thrombin -specific but not factor Xa-specific. The elution peaks at UV 280nm of the protein in the heparin agarose affinity chromatography are in correspondence with the anti-thrombin activity peaks at 405 nm. It can be concluded that the anticoagulant protein isolated from B. kasmiana is thrombin-specific anticoagulant protein. The results of this research lay a foundation for the research of the anticoagulant mechanism and application of anticoagulant protein from B, kasmiana.