Identification of D dimer-E complex in disseminated intravascular coagulation
Whitaker, A.N.; Rowe, E.A.; Masci, P.P.; Gaffney, P.J.
Thrombosis Research 18(3-4): 453-459
1980
ISSN/ISBN: 0049-3848 PMID: 6774434 Document Number: 161934
Serum fibrin degradation products in a patient with severe disseminated intravascular coagulation (caused by fulminant pneumococcal sepsis) were characterized using immunoprecipitation, sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS PAGE) and crossed immunoelectrophoresis. These revealed a spectrum of fragments identified as high MW (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, most of the D dimer and E were noncovalently complexed as D dimer-E and there was relatively little free D dimer and free E. This pattern of FDP (HMW complexes, X and D dimer-E) was 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.