Six monoclonal antibodies raised against human fibrinogen have been characterized. Mouse monoclonal antibodies were targeted against sequential epitopes on the immunodominant D-domain of fibrinogen and they crossreacted with all molecules containing the D-domain [fibrin, fibrin(ogen)-degradation products]. Their behavior was not influenced by proteolytic degradation of fibrinogen with plasmin. Rat MoAbs were specific for the conformational epitopes on intact fibrinogen. Their reactivities were substantially lower with fibrin(ogen)-degradation products. Degradation of structures on intact fibrinogen was concomitant with the decay of rat MoAbs reactivity. Those structures were presumably on the C-terminal end of fibrinogen alpha chain and/or on the N-terminal end of fibrinogen beta chain.

Institute of Haematology and Blood Transfusion Praha Czech Republic

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