Acein‐1, a novel angiotensin‐I‐converting enzyme inhibitory peptide isolated from tryptic hydrolysate of human plasma

FEBS Letters

Tanimura, Takenori¹  Nakagomi, Kazuya¹  Fujii, Noriko²  Fujimura, Akiyoshi¹  Sadakane, Yutaka¹  Sakai, Tomomi¹  Ebisu, Hidetoshi¹ 

[1] Faculty of Pharmaceutical Sciences, Toyama Medical and Pharmaceutical University, 2630 Sugitani, Toyama 930-0194, Japan;PRESTO, JST and Research Reactor Institute, Kyoto University, Kumatori, Sennan, Osaka 590-0494, Japan

关键词: Acein-1;    Angiotensin-I-converting enzyme inhibitor;    Bioactive peptide;    Tryptic hydrolysate;    Human serum albumin;   

DOI  :  10.1016/S0014-5793(98)01311-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A novel angiotensin-I-converting enzyme (ACE) inhibitory peptide, designated acein-1, was isolated from the tryptic hydrolysate of human plasma. Gel filtration and cation exchange chromatography were performed to purify this peptide, followed by reversed-phase gradient and isocratic high-performance liquid chromatography. Acein-1 was found to be a heptapeptide, Tyr-Leu-Tyr-Glu-Ile-Ala-Arg, corresponding to f(138–144) of human serum albumin. The synthetic heptapeptide, hexapeptide (Tyr-Leu-Tyr-Glu-Ile-Ala, des-⁷R acein-1) and octapeptide (Tyr-Leu-Tyr-Glu-Ile-Ala-Arg-Arg, acein-1R) showed dose-dependent inhibitions of ACE, and their IC₅₀ values were 16 μmol/l, 500 μmol/l and 86 μmol/l, respectively. Acein-1 might be a non-competitive inhibitor, while acein-1R may be an uncompetitive inhibitor, as shown by Lineweaver-Burk plots.

【 授权许可】

Unknown