抄録
Analysis was performed on a high-molecular fraction with fibrinogen antigenicity present in Liquid Human Plasma. This fraction, although seemed to resemble macromolecular FDP (fibrinogen degradation product) derived from stabilized fibrin, has many features not shared with the latter:
1) This fraction is sensitive to sodium dodecylsulfate (SDS) treatment.
2) Degradation products of this fraction obtained by digestion with plasmin, when eluted from a column of Sephadex G-200, exhibited a single peak of FDP-D antigenicity at the position of D-monomer.
3) In SDS polyacrylamide gel electrophoresis in the presence of dithiothreitol (DTT), no evidence for the presence of γ-dimer was obtained.
Thus, it is unlikely that the high-molecular fraction is formed through interchain cross-linking between fibrinogen molecules. The formation of the highmolecular complex was discussed in relation to coagulation process in stored plasma.
