Abstract
Circulating crosslinked fibrin was observed in 19 patients with coagulation disorders in obstetrics (amniotic fluid embolism, abruptio placentae, endotoxin shock following septic abortion etc.). Gel filtration of B-Alaprecipitated plasma samples and chain characterization of isolated fibrin derivatives by SDS-PAA gel electrophoresis after reduction with mercaptoethanol were performed. Fibrin was observed in amounts up to 30 mg/100 ml plasma. Subunit structure analysis revealed that circulating fibrin is composed of γ-γ-γ-γ′ (85 000 molecular weight), β, (β′) (52 000 mol. wt.), γ, β″ (44 500 mol. wt.), α (25 000 mol. wt.) and α ″ (15 000 mol. wt.) chains. This composition reflects the action of thrombin, factor XIII and plasmin and agrees with the assumption of γ chain crosslinked late-X oligomers (intermediate polymers). Their mean molecular weight is 1–2 million daltons. Electron microscopy of fibrin following freeze etching technique shows that di-, tri- and higher-ordered oligomers are arranged in an end-to-end association. In vitro produced partially crosslinked oligomers of late-X fragments exhibited a very similar subunit and macromolecular structure.
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