Adelman B, Quynn P
Department of Medicine, Medical College of Virginia, Richmond.
Thromb Haemost. 1989 Dec 29;62(4):1078-82.
This report describes the binding of plasminogen to fibrinogen adsorbed onto polystyrene wells. Binding was determined by enzyme linked immunosorbent assay. Both glu- and lys-plasminogen bound to immobilized fibrinogen in a dose-dependent fashion. However, more lys- than glu-plasminogen bound when equal concentrations of either were added to immobilized fibrinogen. Plasminogen binding was inhibited by epsilon aminocaproic acid indicating that binding was mediated via lysine-binding regions of plasminogen. Soluble fibrinogen added in excess of immobilized fibrinogen did not compete for plasminogen binding but fibrinogen fragments produced by plasmin digestion of fibrinogen did. Treatment of immobilized fibrinogen with thrombin caused a small but significant (p less than 0.01) increase in plasminogen binding. These studies demonstrate that immobilized fibrinogen binds both glu- and lys-plasminogen and that binding is mediated via lysine-binding regions. These interactions may facilitate plasminogen binding to fibrinogen adsorbed on to surfaces and to cells such as platelets which bind fibrinogen.
本报告描述了纤溶酶原与吸附在聚苯乙烯孔上的纤维蛋白原的结合。通过酶联免疫吸附测定法测定结合情况。谷氨酸纤溶酶原和赖氨酸纤溶酶原均以剂量依赖方式与固定化纤维蛋白原结合。然而，当向固定化纤维蛋白原中加入等量的任一种纤溶酶原时，赖氨酸纤溶酶原的结合量比谷氨酸纤溶酶原更多。纤溶酶原的结合受到ε-氨基己酸的抑制，这表明结合是通过纤溶酶原的赖氨酸结合区域介导的。过量添加的可溶性纤维蛋白原不会竞争纤溶酶原的结合，但纤维蛋白原经纤溶酶消化产生的纤维蛋白原片段会竞争。用凝血酶处理固定化纤维蛋白原会导致纤溶酶原结合量有小幅但显著的增加（p小于0.01）。这些研究表明，固定化纤维蛋白原能结合谷氨酸纤溶酶原和赖氨酸纤溶酶原，且结合是通过赖氨酸结合区域介导的。这些相互作用可能有助于纤溶酶原与吸附在表面以及与诸如结合纤维蛋白原的血小板等细胞上的纤维蛋白原结合。
