Fischer-Ferraro C, Nahmod V E, Goldstein D J, Finkielman S
J Exp Med. 1971 Feb 1;133(2):353-61. doi: 10.1084/jem.133.2.353.
An enzyme with the characteristics of classical renin was isolated from brain extracts of nephrectomized dogs. This enzyme is thermolabile, nondialyzable, and forms a vasoconstrictive material when incubated with renin plasma substrate at pH 7. A short lasting pressor activity was also found in brain extracts of dogs and rats. This activity was due to a substance identified by chemical and pharmacological tests as angiotensin. Countercurrent distribution of brain extracts of rats showed that 38% of the pressor activity corresponded to angiotensin II and the remainder to angiotensin I. A remarkable correlation was found between angiotensin and norepinphrine concentrations in different portions of the encephalon of the dog.
从肾切除犬的脑提取物中分离出一种具有经典肾素特性的酶。这种酶不耐热、不可透析,在pH 7条件下与肾素血浆底物孵育时会形成一种血管收缩物质。在犬和大鼠的脑提取物中也发现了短暂的升压活性。这种活性归因于一种经化学和药理学测试鉴定为血管紧张素的物质。大鼠脑提取物的逆流分配显示,38%的升压活性对应于血管紧张素II,其余对应于血管紧张素I。在犬脑不同部位的血管紧张素和去甲肾上腺素浓度之间发现了显著的相关性。