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

Hiroyuki Ukeda, Hiroshi Matsufuji, Toshiro Matsui, Yutaka Osajima, Hideki Matsuda, Katsuhiro Osajima

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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: 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.

Original languageEnglish
Pages (from-to)25-29
Number of pages5
JournalNippon Nogeikagaku Kaishi
Issue number1
Publication statusPublished - Jan 1 1992


All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Food Science
  • Chemistry (miscellaneous)
  • Medicine (miscellaneous)

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