Interaction of Thrombin and Fibrinogen

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Abstract
The author, having described the differences between fibrin and plasma clot, which seem to depend on a "fibrin-stabilizing factor," analyzes how the action of thrombin alters the fibrinogen molecule. Peptides amounting to about 3% of its N content are split off. The associated changes in molecular mass and length are probably too small to measure directly by ordinary physical methods; the molecular weight of the activated fibrinogen must be within a few per cent of the value of 330,000 determined for the parent molecule; and from similar reasoning the molecular length is near 600 A. That the activation causes no gross change in size or shape is borne out by sedimentation, viscosity, and light scattering measurements on dissolved fibrin. However, loss of the peptides causes the net charge (which over most of the pH range of clotting is negative) to become less negative to the extent of 11 to 14 units per molecule, as may be deduced from the composition of the split products as well as differential titration and mobility experiments.

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