THE CLOTTING OF HEMOPHILIC PLASMA BY THROMBOPLASTIC ENZYME

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Abstract
By the addition of pure crystalline trypsin, optimally potentiated by Ca (and cephalin) it is possible to activate the prothrombin of hemophilic globulin substance to normal thrombin and to coagulate hemophilic plasma (in vitro) in manner and extent indistinguishable from the behavior of normal plasma. These facts, together with the author''s experimentally advocated thesis, that phospholipids are normally in firm combination with proteins and, ordinarily, require a trypsin-like enzyme to make them available for an essential role in thrombin formation, suggest that a deficiency of thromboplastic enzyme in the plasma is a logical explanation of the coagulation delay in hemophilia.

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