Nieuwenhuizen W, Verheijen J H, Vermond A, Chang G T
Biochim Biophys Acta. 1983 Feb 22;755(3):531-3. doi: 10.1016/0304-4165(83)90261-1.
Fibrin, in contrast to fibrinogen, strongly accelerates the plasminogen activation by extrinsic activator (tissue-type plasminogen activator, t-PA). However, when fibrin and fibrinogen are digested with cyanogen bromide, both digests potentiate the t-PA-mediated plasminogen activation equally well. In this report, evidence is presented that this potentiating activity resides in CNBr fragment FCB-2 (= Ho1-DSK) and that a polymeric structure such as fibrin is not a prerequisite for the potentiation.
与纤维蛋白原相比，纤维蛋白能强烈加速外源性激活剂（组织型纤溶酶原激活剂，t-PA）介导的纤溶酶原激活。然而，当用溴化氰消化纤维蛋白和纤维蛋白原时，两种消化产物对t-PA介导的纤溶酶原激活的增强作用同样良好。在本报告中，有证据表明这种增强活性存在于溴化氰片段FCB-2（= Ho1-DSK）中，并且诸如纤维蛋白的聚合物结构并非增强作用的先决条件。
