Klechkovskaia V V, Otroshko T A, Egorov N S
Mikrobiologiia. 1979 Sep-Oct;48(5):820-5.
The paper describes some properties of coagulases and fibrinolytic enzymes isolated from a proteolytic complex produced by Aspergillus ochraceus HP-19 during submerged cultivation on a synthetic medium. Proteolytic enzymes with the plasmocoagulating activity hydrolyzed casein at the maximum rate at 45 degrees C and pH 8.0--10.0. The coagulases were stable at pH 5.0--7.0 and were rather resistant to low pH values. The enzymes were entirely inactivated at 55 degrees C within 20--30 min. The activity of the coagulases was inhibited with the ions of Cu, Co, Ag, Pb, Mn, Zn and Hg (1.10(-3) M) by 100, 91, 85, 50, 50, 38 and 25%, respectively. The coagulases were entirely inhibited with EDTA whereas PCMB and PMSF inhibited their activity only to a small extent. The mechanism for blood clotting with the coagulases of Aspergillus ochraceus HP-19 is presumed to consist in the activation of protrombin via its limited specific proteolysis. The fibrinolytic enzymes of Aspergillus ochraceus HP-19 had the optimal pH 8.5 for casein, were stable at pH 6.0, and entirely inactivated at 55 degrees C within 5 min. In contrast to coagulases, they were resistant to the action of heavy metal ions. The enzymes were stabilized by the ions of Ca. The activity of the fibrinolytic enzymes of Aspergillus ochraceus HP-19 was completely inhibited with PMSF. Therefore, they belong to the class of serine proteases.
本文描述了从赭曲霉HP - 19在合成培养基上深层培养产生的蛋白水解复合物中分离出的凝固酶和纤维蛋白溶解酶的一些特性。具有血浆凝固活性的蛋白水解酶在45℃和pH 8.0 - 10.0时以最大速率水解酪蛋白。凝固酶在pH 5.0 - 7.0时稳定，对低pH值有相当的抗性。这些酶在55℃下20 - 30分钟内完全失活。Cu、Co、Ag、Pb、Mn、Zn和Hg（1.10(-3) M）离子分别使凝固酶的活性抑制100%、91%、85%、50%、50%、38%和25%。EDTA可完全抑制凝固酶，而对氯汞苯甲酸和苯甲基磺酰氟仅在小程度上抑制其活性。推测赭曲霉HP - 19的凝固酶使血液凝固的机制在于通过有限的特异性蛋白水解激活凝血酶原。赭曲霉HP - 19的纤维蛋白溶解酶对酪蛋白的最适pH为8.5，在pH 6.0时稳定，在55℃下5分钟内完全失活。与凝固酶不同，它们对重金属离子的作用有抗性。这些酶被Ca离子稳定。赭曲霉HP - 19的纤维蛋白溶解酶的活性被苯甲基磺酰氟完全抑制。因此，它们属于丝氨酸蛋白酶类。
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