FSF‐stabilized soluble fibrinogen/fibrin intermediates in “Ca++‐plasma” at 37 °C

Abstract
Fibrinogen fibrin complexes exist in “Ca+ +‐plasma” (prothrombin‐depleted, Ca+ + boosted, 2.5 mmol/l) adsorbed with Bentonite and enriched with I‐131‐fibrinogen (1.5 mg/ml) and I‐125‐fibrin monomer Des AA (30 μg/ml) at 37 °C. Gel chromatography, in the presence of urea/EDTA, of plasma containing such complexes, which had been enzyme‐linked through the action of 2.5 u/ml plasma XIIIa, demonstrated that fibrin Des AA monomers largely tended to oligomerize (80 per cent of the molecules eluting in front of the 340.000 m.w. species), whereas fibrinogen tended to dimerize and to a smaller extent oligomerize. Furthermore, fibrin Des AA oligomers were partly α‐oligomerized in addition to γγ dimerized, as opposed to fibrinogen which became mainly γγ dimerized.