Pasche B, Kodama K, Larm O, Olsson P, Swedenborg J
Thromb Res. 1986 Dec 15;44(6):739-48. doi: 10.1016/0049-3848(86)90020-4.
About 8000 Daltons porcine mucosa heparin fragments were covalently bonded by end-point attachment to polyethylene. The interaction between the immobilized heparin, added thrombin, and antithrombin III [AT] was investigated. The heparin surface was adsorbed with either albumin, AT dissolved in albumin or Tyrode, or platelet free plasma. Irrespective of the pre-treatment procedure, exposure of the surface to thrombin resulted in the same substantial decrease of thrombin in solution and the same degree of surface-confined thrombin activity. It was concluded that the heparin surface has a large capacity to bind thrombin and that the thrombin inhibitory capacity of high affinity heparin fragments is limited. On exposure of the thrombin-loaded surfaces to defibrinogenated plasma or AT, the surface-confined thrombin was inhibited within 30 seconds. Successive dilutions of plasma or AT decreased the inhibition rate but not the inhibition capacity. It is concluded that inhibition of thrombin adsorbed on the heparin surface occurs as follows: Added AT adheres to high affinity heparin fragments on the surface whereupon adsorbed thrombin migrates in the hydrophilic heparin coating towards the reaction site of AT and becomes inhibited. The inactivated thrombin-AT complex leaves then the surface, thus enabling the process to be repeated.
约8000道尔顿的猪黏膜肝素片段通过终点连接共价结合到聚乙烯上。研究了固定化肝素、添加的凝血酶和抗凝血酶III [AT]之间的相互作用。肝素表面吸附有白蛋白、溶解在白蛋白或台氏液中的AT，或无血小板血浆。无论预处理程序如何，将表面暴露于凝血酶都会导致溶液中凝血酶大幅减少，且表面受限的凝血酶活性程度相同。得出的结论是，肝素表面具有很大的结合凝血酶的能力，且高亲和力肝素片段的凝血酶抑制能力有限。将负载凝血酶的表面暴露于去纤维蛋白血浆或AT后，表面受限的凝血酶在30秒内被抑制。血浆或AT的连续稀释会降低抑制率，但不会降低抑制能力。得出的结论是，对吸附在肝素表面的凝血酶的抑制如下发生：添加的AT附着在表面的高亲和力肝素片段上，随后吸附的凝血酶在亲水性肝素涂层中向AT的反应位点迁移并被抑制。失活的凝血酶-AT复合物然后离开表面，从而使该过程能够重复。
