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Acein‐1, a novel angiotensin‐I‐converting enzyme inhibitory peptide isolated from tryptic hydrolysate of human plasma
Author(s) -
Nakagomi Kazuya,
Fujimura Akiyoshi,
Ebisu Hidetoshi,
Sakai Tomomi,
Sadakane Yutaka,
Fujii Noriko,
Tanimura Takenori
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)01311-8
Subject(s) - hydrolysate , chemistry , human plasma , peptide , enzyme , biochemistry , inhibitory postsynaptic potential , chromatography , hydrolysis , biology , endocrinology
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‐ 7 R acein‐1) and octapeptide (Tyr‐Leu‐Tyr‐Glu‐Ile‐Ala‐Arg‐Arg, acein‐1R) showed dose‐dependent inhibitions of ACE, and their IC 50 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.