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Soluble oligomers of fibrin were produced by limited incubation of fibrinogen with thrombin in the presence of calcium2 positive earth, cysteine and factor XIII. They were separated from fibrinogen by gel filtration. Gamma-gamma dimers were demonstrated in fractions from the void volume and the shoulder prior to the fibrinogen peak. These fractions were subjected to affinity chromatography on agarose-coupled fibrinogen and fibrin. Cross-linked oligomers of fibrin were adsorbed to agarose-coupled fibrin, whereas no adsorption occured during affinity chromatography on agarose-coupled fibrinogen. This indicates that crosslinked fibrin oligomers have no affinity to fibrinogen, yet readily form complexes with fibrin.
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