Taira H, Mizutani S, Narita O, Tomoda Y
Placenta. 1985 Nov-Dec;6(6):543-9. doi: 10.1016/s0143-4004(85)80008-4.
Angiotensin I-converting enzyme (ACE, peptidyldipeptide hydrolase, kininase II, EC 3.4.15.I) from human placenta was purified 6297-fold and characterized. ACE could be extensively purified by affinity chromatography with Captopril (D-3-mercapto-2-methylpropanoyl-L-proline), an orally active antihypertensive agent and a potent inhibitor of this enzyme. Its molecular weight and subunit size were estimated to be 300 000 by high-performance gel permeation chromatography and 85 000 by sodium dodecyl sulphate gel electrophoresis, respectively, indicating its polymeric structure.
从人胎盘中纯化出血管紧张素I转换酶（ACE，肽基二肽水解酶，激肽释放酶II，EC 3.4.15.1），纯化倍数为6297倍，并对其进行了表征。ACE可以通过与卡托普利（D-3-巯基-2-甲基丙酰-L-脯氨酸）进行亲和色谱进行广泛纯化，卡托普利是一种口服活性抗高血压药物，也是该酶的强效抑制剂。通过高效凝胶渗透色谱法估计其分子量为300000，通过十二烷基硫酸钠凝胶电泳法估计其亚基大小为85000，表明其具有聚合结构。
