Fougnot C, Jozefowicz M, Rosenberg R D
Biomaterials. 1984 Mar;5(2):94-9. doi: 10.1016/0142-9612(84)90008-5.
The inhibition of thrombin by antithrombin III is known to be accelerated by heparin through the formation of complexes between the muccopolysaccharide and both proteins. In the preceding papers, we reported that polystyrene derivatives absorb thrombin and its inhibitor with a higher affinity for the protease than for the antiprotease. These complexes are responsible for the catalysis of the generation of thrombin-antithrombin complex which was observed either with purified proteins or in plasma. The protease-antiprotease complex has an affinity for the polymer surface which is higher than that of antithrombin but lower than that of thrombin. Therefore, the thrombin-antithrombin complex generated on the insoluble material is desorbed by thrombin and a catalytic anticoagulant effect can be observed with these polymers.
已知抗凝血酶III对凝血酶的抑制作用会因肝素而加速，这是通过粘多糖与两种蛋白质形成复合物实现的。在之前的论文中，我们报道聚苯乙烯衍生物对凝血酶及其抑制剂具有吸附作用，且对蛋白酶的亲和力高于抗蛋白酶。这些复合物负责催化凝血酶 - 抗凝血酶复合物的生成，这在纯化蛋白质或血浆中均有观察到。蛋白酶 - 抗蛋白酶复合物对聚合物表面的亲和力高于抗凝血酶，但低于凝血酶。因此，在不溶性物质上生成的凝血酶 - 抗凝血酶复合物会被凝血酶解吸，并且可以观察到这些聚合物具有催化性抗凝血作用。
