Peptides from Peptic Hydrolyzate of Heated Sardine Meat That Inhibit Angiotensin I Converting Enzyme.

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  • UKEDA Hiroyuki
    Department of Food Science and Technology, Faculty of Agriculture, Kyushu University
  • MATSUDA Hideki
    Food Research Laboratories, Takara Shuzo Co., Ltd.
  • OSAJIMA Katsuhiro
    Research Laboratories, Senmi Ekisu Co., Ltd.
  • MATSUFUJI Hiroshi
    Department of Food Science and Technology, Faculty of Agriculture, Kyushu University
  • MATSUI Toshiro
    Department of Food Science and Technology, Faculty of Agriculture, Kyushu University
  • OSAJIMA Yutaka
    Department of Food Science and Technology, Faculty of Agriculture, Kyushu University

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Other Title
  • 加熱イワシ筋肉のペプシン加水分解物中に存在するアンジオテンシンＩ変換酵素阻害ペプチド
  • カネツ イワシ キンニク ノ ペプシン カスイ ブンカイブツチュウ ニ ソンザ

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Abstract

Three peptides that inhibited angiotensin I converting enzyme (ACE) were isolated from a peptic hydrolyzate of heated sardine muscle. The preparation involved SP-Sephadex C-25 and Toyopearl HW-40 chromatography followed by three steps of high-performance liquid chromatography. The amino acid sequences of these peptides, identified by Edman degradation, were: B-1, Val-Lys-Ala-Gly-Phe; B-2, Lys-Val-Leu-Ala-Gly-Met; and B-3, Leu-Lys-Leu. The IC50 values of these peptides for ACE from rabbit lung were 83, 30, and 188 μM, respectively. These peptides were synthesized by the solid-phase method, and the IC50 values of the synthetic peptides were similar to those of B-1, B-2, and B-3. These results indicated that all amino acids in B-1, B-2, and B-3 may be in the L-configuration. Fourteen kinds of actins derived from humans, rabbits, rats, mice, soy beans, maize, and so on contained the B-1 sequence of five amino acids.

Journal

  • Nippon Nōgeikagaku Kaishi

    Nippon Nōgeikagaku Kaishi 66 (1), 25-29, 1992

    Japan Society for Bioscience, Biotechnology, and Agrochemistry

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