Department of Bacteriology, School of Medicine, University of Pennsylvania, Philadelphia.
J Gen Physiol. 1937 Mar 20;20(4):543-60. doi: 10.1085/jgp.20.4.543.
Crude or crystalline trypsin in proper concentration causes the blood or plasma of human beings, dogs, rabbits, guinea pigs, and horses to coagulate. It does not clot the fibrinogen directly, but reacts with prothrombin to form thrombin. Since trypsin thus has the same effect as the physiological system Ca plus platelets (or Ca plus tissue extracts), it is suggested as a tentative working hypothesis that the latter system contains a proteolytic enzyme with a specific affinity for prothrombin. Other implications of this trypsin effect with respect to the mechanism of physiological coagulation are discussed in the text (pages 557-558). The proteolytic enzyme papain also coagulates blood. In this case the enzyme does not activate prothrombin, but acts directly on fibrinogen to form a fibrillar gel resembling fibrin. If one admits this clot to be fibrin, this constitutes strong evidence that thrombin, the physiological coagulant, is also a proteolytic enzyme with a specific action on fibrinogen.
在适当浓度下,粗制或结晶胰蛋白酶会使人类、狗、兔、豚鼠和马的血液或血浆发生凝结。它不会直接凝结纤维蛋白原,而是与凝血酶原反应形成凝血酶。由于胰蛋白酶的作用与生理系统中的 Ca 加血小板(或 Ca 加组织提取物)相同,因此可以作为一个试探性的工作假设,即后者系统中含有一种对凝血酶原具有特异性亲和力的蛋白水解酶。本文还讨论了胰蛋白酶对生理凝结机制的其他影响(第 557-558 页)。木瓜蛋白酶也能使血液凝结。在这种情况下,酶不会激活凝血酶原,而是直接作用于纤维蛋白原形成类似于纤维蛋白的纤维状凝胶。如果承认这种凝块是纤维蛋白,这就有力地证明了生理凝血剂凝血酶也是一种对纤维蛋白原具有特异性作用的蛋白水解酶。