FEBS Letters | |
Acein‐1, a novel angiotensin‐I‐converting enzyme inhibitory peptide isolated from tryptic hydrolysate of human plasma | |
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
【 预 览 】
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