源自鲣鱼内脏的血管紧张素I转换酶抑制肽的分离与特性鉴定

Isolation and characterization of angiotensin I-converting enzyme inhibitory peptides derived from bonito bowels.

作者信息

Matsumura N, Fujii M, Takeda Y, Shimizu T

机构信息

Foods Division, Asahi Chemical Industry Co., Ltd., Shizuoka, Japan.

出版信息

Biosci Biotechnol Biochem. 1993 Oct;57(10):1743-4. doi: 10.1271/bbb.57.1743.

DOI:10.1271/bbb.57.1743

PMID:7764272

Abstract

Four angiotensin I-converting enzyme (EC 3.4.15.1) (ACE) inhibitory peptides C105, C107, C111, and C112 were isolated from bonito bowels. C111 was obtained from liver, while the others were from intestine. Their amino acids were sequenced as Ser-Val-Ala-Lys-Leu-Glu-Lys for C105, Ala-Leu-Pro-His-Ala for C107, Gly-Val-Tyr-Pro-His-Lys for C111, and Ile-Arg-Pro-Val-Gln for C112. Their ACE inhibition activities were measured for synthetic peptides. The IC50 of these peptides were estimated to be 82, 79, 1.6, and 1.4 microM, respectively. Carboxyl-terminal amino acid(s) were considered to be essential for their expression of ACE inhibition for C105, C107, and C111, while the amino terminal tripeptide Ile-Arg-Pro of C112 was presumed to inhibit ACE after the removal of a dipeptide from C112 with ACE digestion. Presumed original proteins of these peptides are discussed.

摘要

从鲣鱼内脏中分离出四种血管紧张素I转换酶（EC 3.4.15.1）（ACE）抑制肽C105、C107、C111和C112。C111是从肝脏中获得的，而其他的则来自肠道。它们的氨基酸序列分别为：C105为Ser-Val-Ala-Lys-Leu-Glu-Lys，C107为Ala-Leu-Pro-His-Ala，C111为Gly-Val-Tyr-Pro-His-Lys，C112为Ile-Arg-Pro-Val-Gln。对合成肽测定了它们的ACE抑制活性。这些肽的IC50分别估计为82、79、1.6和1.4微摩尔。对于C105、C107和C111，羧基末端氨基酸被认为对其ACE抑制活性的表达至关重要，而C112的氨基末端三肽Ile-Arg-Pro被推测在经ACE消化从C112去除一个二肽后可抑制ACE。讨论了这些肽的假定原始蛋白质。