Summary
Incubation of fibrinogen with small amounts of thrombin resulted in the occurrence
of soluble fibrin monomer complexes. These complexes consisted predominantly of a
derivative with a higher molecular weight than that of fibrinogen. It was characterized
by its relative electrophoretic mobility in 5% PAA gel (0.28 × 10-5 cm2/V × sec) and its elution position prior to the fibrinogen peak following gel filtration.
Using adsorption chromatography on insolubilized fibrinogen the derivative dissociated
at a ratio of almost 1 : 1 into one part which was adsorbed and into fibrinogen which
was not adsorbed. The part which was adsorbed seemed to be the thrombin mediated fibrin
monomer. This study confirms the concept that dissociable dimeric fibrinogen-fibrin
monomer complexes occur after limited action of thrombin on fibrinogen.