Platelet fibrinogen. Identity and initial observations on the mode of its degradation by plasmin.
Fibrinogen has been purified from human platelets. Platelet fibrinogen exhibits a characteristic pattern in agar gel immunoelectrophoresis different from that of plasma fibrinogen. Stepwise plasmin degradation has been used in further elucidation of the molecular properties of the platelet protein. Examination of comparative digests by immunologic and gel electrophoretic methods has revealed that (1) the platelet protein is more resistant to plasmin degradation, (2) the plasmin-produced fragments of platelet fibrinogen differ consistently from those of its plasma counterpart, and (3) platelet fibrinogen is different from fragment X of plasma fibrinogen. It is suggested that platelet fibrinogen may contribute to the stability of the thrombus.
D000818:Animals; D001780:Blood Coagulation Tests; D001792:Blood Platelets / Q000032:analysis* / Q000276:immunology; D002845:Chromatography; D003636:DEAE-Cellulose; D004591:Electrophoresis, Polyacrylamide Gel; D005340:Fibrinogen / Q000302:isolation & purification; D005341:Fibrinolysin; D006801:Humans; D005779:Immunodiffusion; D007122:Immunoelectrophoresis; D011817:Rabbits / Q000276:immunology
D005340:Fibrinogen; D003636:DEAE-Cellulose; D005341:Fibrinolysin