ANGIOTENSIN I-CONVERTING ENZYME INHIBITORY PEPTIDES DERIVED FROM BONITO BOWELS AUTOLYSATE

被引：79

作者：

MATSUMURA, N ^{[1
]}

FUJII, M ^{[1
]}

TAKEDA, Y ^{[1
]}

SUGITA, K ^{[1
]}

SHIMIZU, T ^{[1
]}

机构：

[1] NIHON SHOKUZAI KAKOU CO LTD, DIV TECH DEV, MIYAZAKI 880, JAPAN

来源：

BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY | 1993年 / 57卷 / 05期

关键词：

D O I：

10.1271/bbb.57.695

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 [生物化学与分子生物学]; 081704 [应用化学];

摘要：

Six angiotensin I-converting enzyme inhibitory peptides were isolated from a bonito bowels autolysate. Their amino acids were sequenced as Tyr-Arg-Pro-Tyr, Gly-His-Phe, Val-Arg-Pro, Ile-Lys-Pro, Leu-Arg-Pro, and Ile-Arg-Pro. Peptides having corresponding amino acid sequences were synthesized by a solid-phase method and their inhibition of the activity measured. IC50 of these peptides were estimated to be 320, 1100, 2.2, 2.5, 1.0, and 1.8 muM, respectively. The role of carboxyl terminal proline residues on the inhibition is discussed.

引用

页码：695 / 697

页数：3

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