Naruse M, Sussman C R, Naruse K, Jackson R V, Inagami T
J Clin Endocrinol Metab. 1983 Sep;57(3):482-7. doi: 10.1210/jcem-57-3-482.
Readily detectable levels of renin activity were demonstrated in human adrenal tissues. This activity was inhibited by specific antibody raised against pure renin, indicating that it was not due to the nonspecific action of proteases. The renin activity was predominantly in the cortex rather than in the medulla of the adrenal. An adrenal gland that was surgically removed from a patient with Cushing's disease and had high renin activity was used for further characterization of the enzyme. It shared many biochemical features with kidney renin, such as molecular weight, isoelectric point, glycoprotein nature, optimum pH of enzyme activity, affinity to pepstatin, and the presence of trypsin-activatable inactive renin. The lack of correlation between PRA and the adrenal renin, and the particulate localization of the subcellular distribution of adrenal renin suggested its local origin rather than contamination or contribution of the plasma enzyme.
在人类肾上腺组织中证实了可轻易检测到的肾素活性水平。这种活性受到针对纯肾素产生的特异性抗体的抑制，这表明它不是由蛋白酶的非特异性作用引起的。肾素活性主要存在于肾上腺皮质而非髓质中。从一名患有库欣病且肾素活性高的患者身上手术切除的一个肾上腺被用于该酶的进一步特性分析。它与肾素在许多生化特性上相同，如分子量、等电点、糖蛋白性质、酶活性的最适pH值、对胃蛋白酶抑制剂的亲和力以及存在可被胰蛋白酶激活的无活性肾素。血浆肾素活性（PRA）与肾上腺肾素之间缺乏相关性，以及肾上腺肾素亚细胞分布的颗粒定位表明其起源于局部而非血浆酶的污染或贡献。
