Kokubu T, Kato I, Nishimura K, Hiwada K, Ueda E
Clin Chim Acta. 1978 Nov 1;89(3):375-9. doi: 10.1016/0009-8981(78)90398-4.
It was demonstrated that angiotensin I-converting enzyme was excreted in human urine. The mean activity of the enzyme in normal urine was found to be 0.38 +/- 0.04 (S.E.M.) units/day (n = 18) and the enzymic activity correlated well with the concentration of the excreted sodium (r = 0.76, p less than 0.005). Urinary angiotensin I-converting enzyme was partially purified. Three different molecular weights of enzyme (greater than 400 000, 290 000 and 140 000) were demonstrated by Sephadex G-200 gel filtration. The enzymic properties of these three enzymes were identical with those of angiotensin I-converting enzyme from human lung with regard to inhibitory effects (bradykinin potentiator c and Arg-Pro-Pro), Cl- dependency, pH optimum and KM value.
已证实血管紧张素I转换酶在人尿中排泄。正常尿液中该酶的平均活性为0.38±0.04（标准误）单位/天（n = 18），酶活性与排泄钠的浓度密切相关（r = 0.76，p＜0.005）。尿血管紧张素I转换酶被部分纯化。通过Sephadex G - 200凝胶过滤证明有三种不同分子量的酶（大于400 000、290 000和140 000）。就抑制作用（缓激肽增强剂c和Arg - Pro - Pro）、Cl - 依赖性、最适pH和KM值而言，这三种酶的酶学性质与来自人肺的血管紧张素I转换酶相同。
