Garman A J, Smith R A
Thromb Res. 1982 Aug 1;27(3):311-20. doi: 10.1016/0049-3848(82)90078-0.
The ability of plasminogen to cause precipitation of soluble fibrin oligomers has been observed and certain features of the phenomenon investigated. The process is mediated by the lysine-binding sites and it appears that at least two such sites are required. Studies using radiolabelled plasminogen revealed that the precipitated material contained fibrin and plasminogen in a 2:1 molar ratio. Further plasminogen molecules are able to bind to the aggregate. The clotting of fibrinogen in the presence of plasminogen was studied using nephelometry. An enhancement by plasminogen of both the rate of clotting and the opacity of the clot was demonstrated. It is proposed that these effects are explicable in terms of a plasminogen-bridging model, in which the zymogen binds divalently between two monomer units of forming polymeric fibrin.
已观察到纤溶酶原可使可溶性纤维蛋白寡聚体沉淀，并对该现象的某些特征进行了研究。该过程由赖氨酸结合位点介导，似乎至少需要两个这样的位点。使用放射性标记的纤溶酶原进行的研究表明，沉淀物质中纤维蛋白和纤溶酶原的摩尔比为2:1。更多的纤溶酶原分子能够结合到聚集体上。使用比浊法研究了纤溶酶原存在下纤维蛋白原的凝血情况。结果表明，纤溶酶原可增强凝血速率和凝块的浊度。有人提出，这些效应可以用纤溶酶原桥接模型来解释，在该模型中，酶原在形成聚合纤维蛋白的两个单体单元之间以二价方式结合。
