Nishimura K, Hiwada K, Ueda E, Kokubu T
Biochim Biophys Acta. 1976 Aug 12;445(1):158-60. doi: 10.1016/0005-2744(76)90168-6.
Approximately 50-fold purification of angiotensin I-converting enzyme (Peptidyldipeptide hydrolase, EC 3.4.15.1) from rabbit lung was achieved by affinity chromatography using the synthetic substrate Hippuryl-His-Leu-OH. The specific activity of the enzyme was increased from 0.044 units/mg protein to 1.911 units/mg protein for Hippuryl-His-Leu-OH and from 0.33 nmol/min per mg protein to 13.8 nmol/min per mg protein for angiotensin I.
利用合成底物马尿酰 - 组氨酰 - 亮氨酸（Hippuryl-His-Leu-OH）通过亲和层析法，实现了从兔肺中对血管紧张素I转换酶（肽基二肽水解酶，EC 3.4.15.1）约50倍的纯化。对于马尿酰 - 组氨酰 - 亮氨酸，该酶的比活性从0.044单位/毫克蛋白质提高到1.911单位/毫克蛋白质；对于血管紧张素I，比活性从每毫克蛋白质0.33纳摩尔/分钟提高到每毫克蛋白质13.8纳摩尔/分钟。
