Veremeenko K N, Kizim A I, Lositskaia V M
Vopr Med Khim. 1977 May-Jun(3):391-6.
The nature of protamine splitting proteinase, which was formed after treatment of human blood plasma by kaolin or silicone (aerosile), was studied. The activated enzyme did not exhibite the properties of thrombin and plasmin in reactions with specific substrates. Kyninogenic, TAME (N-tosyl-d-,l-arginine methyl ester)-esterase and protamine splitting activities were inherent in the proteinase; these properties enabled to group the enzyme with blood kallikreins. The purified preparations of human blood plasma kallikrein hydrolyzed protamine sulphate even at 10 mcg/ml concentration. alpha2-macroglobulin inhibited the protamine splitting activity of the plasma kallikrein.
研究了用高岭土或硅酮（气雾剂）处理人血浆后形成的鱼精蛋白裂解蛋白酶的性质。该活化酶在与特定底物反应时不表现出凝血酶和纤溶酶的特性。该蛋白酶具有激肽原生成、TAME（N-对甲苯磺酰-d，l-精氨酸甲酯）酯酶和鱼精蛋白裂解活性；这些特性使该酶可归类于血液激肽释放酶。人血浆激肽释放酶的纯化制剂即使在浓度为10微克/毫升时也能水解硫酸鱼精蛋白。α2-巨球蛋白抑制血浆激肽释放酶的鱼精蛋白裂解活性。
