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通过亲和色谱法从蛋白酶中分离出大鼠脑中肾素的确切证据。

Definitive evidence for renin in rat brain by affinity chromatographic separation from protease.

作者信息

Inagami T, Yokosawa H, Hirose S

出版信息

Clin Sci Mol Med Suppl. 1978 Dec;4:121s-123s. doi: 10.1042/cs055121s.

Abstract
  1. Angiotensin I-generating activity of rat brain extract was separated into two components by affinity chromatography on a casein-Sepharose gel column. 2. The component without affinity to the gel was identified as true renin on the basis of its sensitivity to anti-renin antibody and the lack of protease activity. 3. The second renin-like component with affinity to the gel was a protease insensitive to the anti-renin antibody. Its renin-like activity examined with sheep substrate was pronounced compared with the rate of angiotensin I generation from the rat substrate. 4. It was concluded that rat brain contains true renin, which can be detected by the use of rat substrate but can be masked when examined with sheep substrate.
摘要
  1. 通过在酪蛋白-琼脂糖凝胶柱上进行亲和层析,将大鼠脑提取物的血管紧张素I生成活性分离为两个组分。2. 基于其对抗肾素抗体的敏感性和缺乏蛋白酶活性,将对凝胶无亲和力的组分鉴定为真性肾素。3. 第二个与凝胶有亲和力的类肾素组分是一种对抗肾素抗体不敏感的蛋白酶。与从大鼠底物生成血管紧张素I的速率相比,用绵羊底物检测时其类肾素活性明显。4. 得出的结论是,大鼠脑含有真性肾素,使用大鼠底物时可检测到,但用绵羊底物检测时可能会被掩盖。

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