Heene D L, Matthias F R, Wegrzynowicz Z, Hocke G
Thromb Haemost. 1979 Jun 30;41(4):677-86.
The phenomenon of complex formation between fibrinmonomer and fibrinogen degradation products was investigated by means of adsorption of FDP to insolubilized thrombin-modified fibrinogen (FM-ag). Since it could be demonstrated that there are different adsorption characteristics for early FDP and late FDP, the possibility of separation of FDP by means of affinity chromatography on FM-ag columns was evaluated using plasmic digests of 3H-Ac-labelled fibrinogen. The identification of FDP was performed by disc-electrophoresis. The results indicate that the adsorption of early FDP is comparable to the behaviour of fibrinogen, whereas late FDP show essential difference in the affinity towards FM-ag, evident by the result that fragment E adsorbs only to a minimal extents. Fragments D and E derived from fibrinogen as well as from non-crosslinked fibrin, revealed identical adsorption characteristics. Under specified conditions the procedure is suitable as a preparative method for the separation of fragments D and E.
通过将纤维蛋白原降解产物（FDP）吸附到不溶性凝血酶修饰的纤维蛋白原（FM-ag）上，研究了纤维蛋白单体与FDP之间形成复合物的现象。由于已证明早期FDP和晚期FDP具有不同的吸附特性，因此使用3H-乙酰基标记的纤维蛋白原的血浆消化物，评估了在FM-ag柱上通过亲和色谱法分离FDP的可能性。通过圆盘电泳对FDP进行鉴定。结果表明，早期FDP的吸附与纤维蛋白原的行为相当，而晚期FDP对FM-ag的亲和力则存在本质差异，片段E仅在最小程度上吸附这一结果就很明显。源自纤维蛋白原以及非交联纤维蛋白的片段D和E显示出相同的吸附特性。在特定条件下，该方法适合作为分离片段D和E的制备方法。
