Marsh N A
Thromb Haemost. 1979 Aug 31;42(2):757-63.
The fibrinogen molecule has a number of biological activities and some of these are shared by the larger degradation products. This study was carried out to investigate the erythrocyte sedimentation-accelerating property of fibrinogen and how this property might be modified by proteolytic digestion with plasmin. The sedimentation rate of washed human red cells suspended in saline, was found to be directly proportional to the concentration of added purified human fibrinogen, down to 250 mg%, below which there was no difference from saline controls. Plasmic digestion of fibrinogen yielding fragment X, did not reduce the accelerating affect on erythrocyte sedimentation, indicating that the intact carboxyl terminal end of the A alpha chain is unnecessary for this phenomenon. Further digestion to fragment Y reduced the effect slightly but digestion to fragments D and E abolished the accelerating effect completely.
纤维蛋白原分子具有多种生物学活性，其中一些较大的降解产物也具有这些活性。本研究旨在探讨纤维蛋白原的促红细胞沉降特性，以及纤溶酶的蛋白水解消化如何改变这种特性。结果发现，悬浮在盐水中的洗涤过的人红细胞的沉降率与添加的纯化人纤维蛋白原的浓度成正比，低至250mg%，低于此浓度则与盐水对照组无差异。纤维蛋白原经纤溶酶消化产生片段X，对红细胞沉降的加速作用并未降低，这表明Aα链完整的羧基末端对此现象并非必需。进一步消化成片段Y，作用略有降低，但消化成片段D和E则完全消除了加速作用。
