Summary
Chromatographed thrombin in the presence of both 50 Kallikrein inhibitor units of
Trasylol per ml and 0.1 M E-ACA solubilized fibrin and the products of lysis possessed
anticoagulant properties. The peak of the antithrombic activity coincided with the
time of complete lysis of the fibrin clot, plasmin lysed fibrin exhibited the peak
of its antithrombic activity much earlier. The effect of thrombin lysed fibrin on
the prothrombin consumption of shed blood was found to be inhibitory.
The products of the digestion of fibrin by thrombin and by plasmin, isolated at an
advanced stage of proteolysis were compared by gel filtration, disc electrophoresis
and DEAE cellulose chromatography. Differences in physical characteristics of these
fibrin breakdown products offer evidence that they were produced by two different
enzymes.