Loginov A V, Fateeva L I
Antibiot Khimioter. 1988 Jun;33(6):436-40.
Carboxyl proteinase (CP) with the isoelectric point of 6.3-6.4 was isolated from a fungus at the Laboratory of Enzymology of the All-Union Research Technological Institute of Antibiotics and Enzymes and its effect on the kallikrein-kinin system and trypsin caseinolytic activity was studied. Four lots of the preparation with the activity of 1116 to 2300 milk coagulating units per 1 mg were used. The kininogenase activity of kallikrein, bradykinin and trypsin was determined with the routine biological procedures and the trypsin caseinolytic activity was determined with the Kunitz method and the diffusion method on casein-containing agar. It was shown that CP inhibited the kininogenase activity of kallikrein in the secretion of the salivary glands of man and crystalline trypsin in aqueous media and blood serum. It also inactivated the bradykinin constrictor effect on the smooth muscle tissue of the uterus horn in rats. CP had a capacity for inhibiting the caseinolytic activity of crystalline trypsin. Possible use of CP in treatment of patients with diseases accompanied by impairment of the kallikrein-kinin system (increased activity) is discussed.
在全苏抗生素与酶研究技术研究所酶学实验室从一种真菌中分离出了等电点为6.3 - 6.4的羧基蛋白酶（CP），并研究了其对激肽释放酶 - 激肽系统及胰蛋白酶酪蛋白水解活性的影响。使用了4批每1毫克活性为1116至2300个凝乳单位的制剂。采用常规生物学方法测定激肽释放酶、缓激肽和胰蛋白酶的激肽原酶活性，用库尼茨法和含酪蛋白琼脂扩散法测定胰蛋白酶酪蛋白水解活性。结果表明，CP在人唾液腺分泌物及水介质和血清中的结晶胰蛋白酶中抑制激肽释放酶的激肽原酶活性。它还使缓激肽对大鼠子宫角平滑肌组织的收缩作用失活。CP有抑制结晶胰蛋白酶酪蛋白水解活性的能力。讨论了CP在治疗伴有激肽释放酶 - 激肽系统受损（活性增加）疾病患者中的可能用途。
