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We generated in vitro fibrinogen degradation products (FDP) and determined which fibrinogen (Fg) fragments could be detected by E-neoantigen radioimmunoassay (RIA). Rabbits were immunized with fragment E derived from the plasmin cleavage of Fg, and the anti-Fg-E sera were absorbed with native Fg. The absorbed antisera contained antibodies which reacted with Fg-E (but not with Fg) and its related FDP via neoantigenic expression of Fg-E (Fg-Eneo). Fg was digested by urokinase-activated plasminogen at 37°C for varying periods from 5 min to 16 hr. A double antibody RIA using anti-Fg-Eneo and an 125I-Fg-E tracer showed progressive exposure of Eneo after digesting Fg for 2 hr (fragment X). The inhibition curve of the 4 hr-digest (fragment Y) exhibited a parrellism to that of Fg-E standard; however, the 50% inhibition point of the 4 hr-digest was noticeably displaced. According to Scatcherd plots of the bound/free ratio of Fg-absorbed and unabsorbed anti- Fg-E, both anti-Fg-E and anti-Fg-Eneo contained antibodies that were heterogeneous. These findings suggest that radioimmunologically Y (but not X) fragments were detected as identical molecular species of Fg-E. The Eneo will also be generated in plasma by urokinase-activated plasminogen. The reaction between anti-Fg-Eneo and X, Y or E fragment will be inhibited by timed plasmin digests.

In Vitro Generation Of E-Neoantigen Measured By Radioimmunoassay