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Homogenized fibrin induced platelet aggregation and the release of serotonin from human platelets. Fragment D, purified from a plasmin digest of human fibrinogen, inhibited these platelet-fibrin interactions. Using a radiolabeled fragment D, it was possible to demonstrate saturable binding of fragment D to fibrin. Nonlabeled fragment D competed with the radiolabeled fragment D for binding to fibrin. Furthermore, the binding of fragment D to fibrin paralleled its ability to inhibit the fibrin-induced release of platelet serotonin. It is postulated that the inhibitory effect of fragment D on fibrin activation of platelets is due to the binding of fragment D to fibrin. The bound fragment D may cover up or block sites on fibrin that are involved in fibrin-platelet interactions. This would then result in inhibition of the fibrin-induced platelet aggregation and release of platelet serotonin.
K G Orloff, and
D Michaeli
September 1981,
The Biochemical journal,
K G Orloff, and
D Michaeli
January 2013,
Methods in molecular biology (Clifton, N.J.),
K G Orloff, and
D Michaeli
August 1980,
Thrombosis research,
K G Orloff, and
D Michaeli
October 1980,
Biokhimiia (Moscow, Russia),
K G Orloff, and
D Michaeli
November 1989,
Proceedings of the National Academy of Sciences of the United States of America,
K G Orloff, and
D Michaeli
July 2020,
Blood advances,
K G Orloff, and
D Michaeli
April 1976,
British journal of obstetrics and gynaecology,
K G Orloff, and
D Michaeli
February 1970,
Thrombosis et diathesis haemorrhagica,
K G Orloff, and
D Michaeli
January 1975,
Texas reports on biology and medicine,
K G Orloff, and
D Michaeli
July 1973,
The Journal of biological chemistry,
