Nolly H, Bertini F, Lama M C
Adv Exp Med Biol. 1983;156:399-407.
The present study was undertaken to examine whether there is a kallikrein-like enzyme in vascular tissue. Isolated saline-perfused rat mesenteric arteries were used. A kallikrein-like enzyme and acid protease from saline-perfused mesenteric arteries were separated by CM-cellulose chromatography with a linear NaCl gradient. The separation made it possible to study the optimum pH of the kallikrein-like enzyme and acid protease. The kallikrein-like enzyme showed optimal activity in the range of pH 7-9 and the acid protease in the range of pH 4-5. Both enzymes when acting on a protein plasma substrate release an active peptide that has a similar chemical and pharmacological properties to bradykinin. Using antibodies that specifically inhibit kinins, the biological action was completely abolished. These results indicate that arterial tissue contains two enzymes which generate kinins, the characteristics of one of the enzymes are quite similar to those of a lysosomal protease of the cathepsin-like type of enzyme and the other differs clearly from the acid protease and plasma kallikreins and has physicochemical characteristics quite similar to those of the kallikreins of glandular origin.
本研究旨在检测血管组织中是否存在类激肽释放酶。采用分离的经生理盐水灌注的大鼠肠系膜动脉。用线性NaCl梯度的CM - 纤维素色谱法分离经生理盐水灌注的肠系膜动脉中的类激肽释放酶和酸性蛋白酶。该分离方法使得研究类激肽释放酶和酸性蛋白酶的最适pH成为可能。类激肽释放酶在pH 7 - 9范围内表现出最佳活性，酸性蛋白酶在pH 4 - 5范围内表现出最佳活性。两种酶作用于蛋白质血浆底物时都会释放出一种活性肽，该活性肽具有与缓激肽相似的化学和药理特性。使用特异性抑制激肽的抗体，生物活性完全被消除。这些结果表明动脉组织含有两种产生激肽的酶，其中一种酶的特性与组织蛋白酶样类型的溶酶体蛋白酶非常相似，另一种则明显不同于酸性蛋白酶和血浆激肽释放酶，其理化特性与腺源性激肽释放酶非常相似。
