Abstract
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 α chain and/or on the N-terminal end of fibrinogen β chain.
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