Angiotensin I-converting Enzyme Inhibitory Peptides in an Alkaline Protease Hydrolyzate Derived from Sardine Muscle

Hiroshi Matsufuji, Toshiro Matsui, Masatoshi Nakashima, Yutaka Osajima, Eiji Seki, Katsuhiro Osajima

研究成果: Contribution to journalArticle査読

220 被引用数 (Scopus)

抄録

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 100μM of IC50 value; the maximal inhibitory activity was observed for Lys-Trp (IC50 = 1.63 μm). 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 Asp[l]-angiotensin I.

本文言語英語
ページ(範囲)2244-2245
ページ数2
ジャーナルBioscience, biotechnology, and biochemistry
58
12
DOI
出版ステータス出版済み - 1994

All Science Journal Classification (ASJC) codes

  • バイオテクノロジー
  • 分析化学
  • 生化学
  • 応用微生物学とバイオテクノロジー
  • 分子生物学
  • 有機化学

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