In a careful study of the properties of the proteolytic enzyme of plasma which is active near neutrality, Christensen (1) reported that preparations of this substance digested fibrinogen and fibrin with equal avidity. This observation has been challenged by Fantl, Simon, and Fitzpatrick (2,3) who claimed that fibrin is a more suitable substrate for this enzyme than fibrinogen.The experiments to be described were undertaken to investigate these two divergent views. The problem to be resolved necessitated a comparison between the time required for the digestion of two different proteins, fibrinogen and fibrin. Fantl and his associates (2, 3) measured the digestion of fibrin by observing the time required for the lysis of the fibrin clot. They studied the digestion of fibrinogen by measuring the amount of this protein which was clotted by thrombin or calcium after an appropriate period of incubation. Under the conditions of their experiments, these workers observed that the fibrin clot was liquefied at a time when appreciable amounts of coagulable fibrinogen remained in the unclotted control mixtures.In Christensen's experiments, the rate of proteolysis of fibrinogen and of fibrin was determined by measuring the amount of nitrogen in the precipitate which formed upon the addition of trichloracetic acid (1). With this method it was not feasible to determine the rate of digestion of fibrin until lysis of the clot had occurred, but thereafter fibrinolysis and fibrinogenolysis appeared to proceed at the same rate.