Acein-1, a novel angiotensin-I-converting enzyme inhibitory peptide isolated from tryptic hydrolysate of human plasma
作者： Kazuya Nakagomi , Akiyoshi Fujimura , Hidetoshi Ebisu , Tomomi Sakai , Yutaka Sadakane
DOI: 10.1016/S0014-5793(98)01311-8
关键词:
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 followed by reversed-phase gradient isocratic high-performance liquid chromatography. Acein-1 found be a heptapeptide, Tyr-Leu-Tyr-Glu-Ile-Ala-Arg, corresponding f(138–144) serum albumin. The synthetic hexapeptide (Tyr-Leu-Tyr-Glu-Ile-Ala, des-7R acein-1) octapeptide (Tyr-Leu-Tyr-Glu-Ile-Ala-Arg-Arg, acein-1R) showed dose-dependent inhibitions ACE, their IC50 values 16 μmol/l, 500 μmol/l 86 respectively. might non-competitive inhibitor, while acein-1R may an uncompetitive as shown Lineweaver-Burk plots.
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