Summary
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 extent. 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.