Otokida K, Nakamura M, Kawamura K, Kanazawa S, Kato M
Tohoku J Exp Med. 1984 Sep;144(1):91-101. doi: 10.1620/tjem.144.91.
The angiotensin converting enzyme (ACE) activity in the plasma collected from normotensive and hypertensive patients was measured chromatographically by two different methods using hippuryl-histidyl-leucine (HHL-ACE) and synthetic angiotensin I (AI-ACE) as substrates. A single peak was observed in the elution profiles of HHL-ACE on both Sephadex G 150 column and DEAE Sephadex A 50 cellulose column chromatographies. A single peak of AI-ACE appeared on the gel-filtration. However, several peaks of AI-ACE were seen on DEAE Sephadex A 50 cellulose column chromatography, suggesting that there are various types of ACE which hydrolyze angiotensin I but not HHL.
采用两种不同的色谱法，分别以马尿酰 - 组氨酰 - 亮氨酸（HHL - ACE）和合成血管紧张素I（AI - ACE）为底物，测定了从血压正常和高血压患者采集的血浆中血管紧张素转换酶（ACE）的活性。在Sephadex G 150柱和DEAE Sephadex A 50纤维素柱色谱上，HHL - ACE的洗脱图谱均观察到一个单一峰。在凝胶过滤中出现了AI - ACE的一个单一峰。然而，在DEAE Sephadex A 50纤维素柱色谱上可见多个AI - ACE峰，这表明存在多种能水解血管紧张素I但不能水解HHL的ACE类型。
