Kinin-forming enzyme (kininogenin) in homogenates of rat kidney

Ivan F. Carvalho, Carlos R. Diniz
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引用次数: 28

Abstract

An enzyme has been found in rat-kidney homogenates with the ability to release bradykinin or related peptides from plasma globulin. The system is normally inactive but can easily be activated in hypotonic media at pH 5.0.

Centrifugation studies have shown that most of the enzymatic activity is concentrated in particles with the sedimentation characteristics of lysosomes or droplets.

The sediment is inactive and can be activated by procedures used to release phosphate from lysosomes.

The kidney enzyme has many properties of the urinary kallikrein found in rat urine.

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大鼠肾匀浆中的激肽形成酶(激肽原)
在大鼠肾匀浆中发现一种酶能够从血浆球蛋白中释放缓激肽或相关肽。该系统通常不活跃,但在pH 5.0的低渗介质中很容易被激活。离心研究表明,大部分酶活性集中在具有溶酶体或液滴沉降特性的颗粒中。沉积物是无活性的,可以通过从溶酶体释放磷酸盐的程序来激活。肾酶具有在大鼠尿液中发现的尿钾激肽的许多特性。
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