Preparations of human fibrinogen, digested by plasmin, inhibited ADP induced platelet aggregation; the inhibitory activity was confined to the small dialyzable fragments accumulating during the degradation. Purified large molecular weight fragments D and E had no effect on ADP induced aggregation, but fragment E inhibited thrombin induced aggregation. Extensively degraded bovine fibrinogen preparations also inhibited platelet aggregation by ADP. Both human and bovine fibrinogen preparations were contaminated with factor VIII related material (factor VIII related antigen and factor VIII procoagulant activity, respectively); separation of factor VIII related material from human or bovine fibrinogen by gel chromatography and subsequent plasmin digestion of the fractions revealed that the inhibitory activity was mainly linked to digested factor VIII related material. This inhibitory activity was dialyzable. The effect of fibrinogen digests on platelet aggregation should therefore be reconsidered.
|Number of pages||7|
|Publication status||Published - 1974|
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