Yokosawa N, Takahashi N, Inagami T, Page D L
Biochim Biophys Acta. 1979 Aug 15;569(2):211-9. doi: 10.1016/0005-2744(79)90056-1.
Existing views on prorenin are conflicting and its physiological activation mechanism is not clear. In an attempt to obtain clearcut views on the molecular properties of prorenin in human plasma, the renin zymogen (prorenin) was separated from active renin by two steps of affinity chromatography and it was demonstrated that prorenin is a completely inactivate zymogen contrary to the existing information. Inactive prorenin has an apparent molecular of 56,000 contrary to 46,000-43,000 of partially active prorenin. Isolated and acid-treated human prorenin was shown to be activated by kallikreins from human urine and plasma. This activation was completely blocked by Trasylol. Hog pancreatic kallikrein also activated human prorenin. The kallikrein mediated activation of prorenin indicates the existence of a new link between the vasoconstricting renin-angiotensin system and the vasodilating kallikreinkinin system.
目前关于肾素原的观点相互矛盾，其生理激活机制尚不清楚。为了明确人血浆中肾素原的分子特性，通过两步亲和层析法将肾素酶原（肾素原）与活性肾素分离，并证明肾素原是一种完全无活性的酶原，这与现有信息相反。无活性肾素原的表观分子量为56,000，而部分活性肾素原的分子量为46,000 - 43,000。分离并经酸处理的人肾素原可被人尿液和血浆中的激肽释放酶激活。这种激活被抑肽酶完全阻断。猪胰激肽释放酶也能激活人肾素原。激肽释放酶介导的肾素原激活表明血管收缩性肾素 - 血管紧张素系统与血管舒张性激肽释放酶 - 激肽系统之间存在新的联系。
