Kinin-forming enzymes in vascular tissue.
Kinin-forming enzymes in vascular tissue.
复制标题
血管组织中的激肽形成酶。
DOI：
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发表时间：
1983
影响因子：
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通讯作者：
M. Lama
中科院分区：
文献类型：
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作者：
H. Nolly;F. Bertini;M. Lama
本研究旨在探讨血管组织中是否存在激肽释放酶样酶。采用离体盐水灌注大鼠肠系膜动脉。从盐水灌注的肠系膜动脉的激肽释放酶样酶和酸性蛋白酶分离CM-纤维素色谱与线性NaCl梯度。分离使得研究激肽释放酶样酶和酸性蛋白酶的最佳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。当作用于蛋白质血浆底物时，两种酶释放具有与缓激肽相似的化学和药理学性质的活性肽。使用特异性抑制激肽的抗体，生物作用被完全消除。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酶的溶酶体蛋白酶的特性非常相似，另一种酶与酸性蛋白酶和血浆激肽释放酶明显不同，并且具有与腺源性激肽释放酶非常相似的理化特性。
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.