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来自清酒及酒粕的血管紧张素I转换酶抑制肽的结构与活性

Structure and activity of angiotensin I converting enzyme inhibitory peptides from sake and sake lees.

作者信息

Saito Y, Wanezaki K, Kawato A, Imayasu S

机构信息

Research Institute, Gekkeikan Sake Co., Ltd., Kyoto, Japan.

出版信息

Biosci Biotechnol Biochem. 1994 Oct;58(10):1767-71. doi: 10.1271/bbb.58.1767.

DOI:10.1271/bbb.58.1767
PMID:7765503
Abstract

Nine peptides to inhibit angiotensin I converting enzyme (ACE) were isolated from sake and sake lees. They were short peptides with 5 or fewer amino acid residues, and many of them had a tryptophan or tyrosine residue at the C-terminus. We synthesized the peptide fragments of IYPRY and YGGY, and measured their inhibitory activity. As a result, we have concluded that hydrophobic amino acids in the sequence and amino acid at C-terminus had an important role in the inhibition. When digested with pepsin and pancreatin, YGGY lost its inhibitory activity but IYPRY maintained its activity. YGGY and IYPRY were orally administered to spontaneously hypertensive rats (SHR) at the dose of 100 mg/kg. YGGY didn't change the blood pressure of SHR, but IYPRY reduced their blood pressure. The hypotensive effect of IYPRY continued for 30 h after administration. Also, three dipeptides among the IYPRY fragments, IY, YP and RY, had hypotensive effects, and the effect of RY continued for 30 h after administration.

摘要

从清酒和酒粕中分离出9种抑制血管紧张素I转换酶(ACE)的肽。它们是氨基酸残基为5个或更少的短肽,其中许多在C端含有色氨酸或酪氨酸残基。我们合成了IYPRY和YGGY的肽片段,并测定了它们的抑制活性。结果,我们得出结论,序列中的疏水氨基酸和C端的氨基酸在抑制中起重要作用。用胃蛋白酶和胰酶消化后,YGGY失去了抑制活性,但IYPRY保持了其活性。以100mg/kg的剂量将YGGY和IYPRY口服给予自发性高血压大鼠(SHR)。YGGY没有改变SHR的血压,但IYPRY降低了它们的血压。IYPRY的降压作用在给药后持续30小时。此外,IYPRY片段中的三种二肽IY、YP和RY具有降压作用,RY的作用在给药后持续30小时。

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