Identification of D dimer-E complex in disseminated intravascular coagulation

Abstract

Serum fibrin degradation products in a patient with severe disseminated intravascular coagulation (caused by fulminant pneumococcal sepsis), were characterized using immunoprecipitation, sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS PAGE) and crossed immunoelectrophoresis. These revealed a spectrum of fragments identified as high molecular weight (HMW) complexes, a component with mobility on SDS PAGE similar to that of fibrinogen X (“X”), D dimer and E. By their electrophoretic characteristics and reactions with antisera to fragments E and D it was found that most of the D dimer and E were noncovalently complexed as D dimer-E, and that there was relatively little free D dimer and free E. This pattern of FDP (HMW complexes, “X” and D dimer-E) has also been identified during the lysis of crosslinked fibrin by plasmin. The HMW complexes and “X” are believed to be crosslinked X oligomers and crosslinked Y-Y or Y-D respectively.