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A murine monoclonal antibody (anti-C2G7), reactive with fibrinogen, was used to analyse the structure and function of the fibrinogen epitope C2G7. Anti-C2G7 was found to be reactive with fibrinogen but not with fibronectin, Factor VIII-von Willebrand Factor (FVIII-vWF), beta-thromboglobulin (beta TG), platelet factor 4 (PF4) nor with a range of normal cells and cell lines. Biochemical and plasmin digestion studies of fibrinogen revealed that C2G7 is present on the carboxy-terminal end of the alpha chain on a fragment with a Mr approximately 30-40 K. Functional studies, on the role of fibrinogen in coagulation and platelet function, demonstrated the importance of C2G7 (or a closely associated region) for thrombin-associated fibrin polymerization and collagen induced fibrinogen binding to platelets. |
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