源自沙丁鱼肌肉的碱性蛋白酶水解物中的血管紧张素I转换酶抑制肽。

Angiotensin I-converting enzyme inhibitory peptides in an alkaline protease hydrolyzate derived from sardine muscle.

作者信息

Matsufuji H, Matsui T, Seki E, Osajima K, Nakashima M, Osajima Y

机构信息

Department of Food Science and Technology, Faculty of Agriculture, Kyushu University, Fukuoka, Japan.

出版信息

Biosci Biotechnol Biochem. 1994 Dec;58(12):2244-5. doi: 10.1271/bbb.58.2244.

DOI:10.1271/bbb.58.2244

PMID:7765718

Abstract

The ACE inhibitory activity of an alkaline protease hydrolyzate from sardine muscle did not change after being treated by gastrointestinal proteases (IC50 = 0.082 mg protein/ml). Eleven new ACE inhibitory peptides, constructed with 2 to 4 amino acid residues, were isolated from the hydrolyzate. The ACE inhibitory activity of each was mostly below 100 microM of IC50 value; the maximal inhibitory activity was observed for Lys-Trp (IC50 = 1.63 microM). The isolated peptides inhibited ACE competitively, except for Met-Tyr with non-competitive inhibition. As the result of sequence homology, Arg-Val-Tyr isolated from the hydrolyzate was found in the primary structure of angiotensins I, II, and III, and of des As[1]-angiotensin I.

摘要

沙丁鱼肌肉碱性蛋白酶水解产物经胃肠蛋白酶处理后，其ACE抑制活性未发生变化（IC50 = 0.082 mg蛋白/ml）。从该水解产物中分离出11种由2至4个氨基酸残基组成的新型ACE抑制肽。每种肽的ACE抑制活性大多低于100 μM的IC50值；Lys-Trp的抑制活性最高（IC50 = 1.63 μM）。除了具有非竞争性抑制作用的Met-Tyr外，分离出的肽对ACE具有竞争性抑制作用。序列同源性分析结果表明，从水解产物中分离出的Arg-Val-Tyr存在于血管紧张素I、II和III以及去As[1]-血管紧张素I的一级结构中。