Isolation of Acein‐2, a novel angiotensin‐I‐converting enzyme inhibitory peptide derived from a tryptic hydrolysate of human plasma

FEBS Letters

Akizawa, Toshifumi²  Tanimura, Takenori¹  Nakagomi, Kazuya¹  Sadakane, Yutaka¹  Yamada, Riho¹  Ebisu, Hidetoshi¹ 

[1] Faculty of Pharmaceutical Sciences, Toyama Medical and Pharmaceutical University, 2630 Sugitani, Toyama 930-0194, Japan;Faculty of Pharmaceutical Sciences, Setsunan University, 45-1 Nagaotoge-cho, Hirakata 570-0101, Japan

关键词: Acein-2;    Acein-1;    Angiotensin-I-converting enzyme inhibitory peptide;    Tryptic hydrolysate;    Human α2-macroglobulin;   

DOI  :  10.1016/S0014-5793(00)01163-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

We previously described a novel angiotensin-I-converting enzyme (ACE) inhibitory peptide, designated Acein-1, that was isolated from a tryptic hydrolysate of human plasma. We now report a second such inhibitory peptide, Acein-2 obtained from the same hydrolysate. The peptide was purified by gel filtration and cation exchange chromatography followed by reversed-phase gradient and isocratic high performance liquid chromatography. Acein-2 was found to be a tripeptide, Leu-Ile-Tyr, which is thought to correspond to f(518–520) of human α2-macroglobulin. The synthetic tripeptide showed a potent dose-dependent inhibition of ACE, with an IC₅₀ value of 0.82 μmol/l. Lineweaver–Burk plots suggested that Acein-2 as well as the previously described Acein-1 are non-competitive inhibitors.

【 授权许可】

Unknown