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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 anticoagulant proteins were isolated from the crude extract of Batracobdellakasmiana by ultracentrifugation and heparin agarose affinity chromatography. The anticoagulant activity test demonstrated that these two proteins had a significant inhibition of thrombin activity but did not inhibit the activity of factor Xa. The protein elution peak of affinity chromatography is consistent with the activity peak of thrombin inhibition; therefore, the anti-coagulant protein of frog tadpole is an anti-coagulant protein specific to thrombin. This lays the foundation for the further study of the anticoagulant mechanism of anti-clotting protein in the frog tadpole and its application.