Abstract
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.
| Original language | English |
|---|---|
| Pages (from-to) | 2244-2245 |
| Number of pages | 2 |
| Journal | Bioscience, Biotechnology, and Biochemistry |
| Volume | 58 |
| Issue number | 12 |
| DOIs | |
| Publication status | Published - Jan 1 1994 |
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All Science Journal Classification (ASJC) codes
- Biotechnology
- Analytical Chemistry
- Biochemistry
- Applied Microbiology and Biotechnology
- Molecular Biology
- Organic Chemistry
Cite this
Angiotensin I-converting Enzyme Inhibitory Peptides in an Alkaline Protease Hydrolyzate Derived from Sardine Muscle. / Matsufuji, Hiroshi; Matsui, Toshiro; Nakashima, Masatoshi; Osajima, Yutaka; Seki, Eiji; Osajima, Katsuhiro.
In: Bioscience, Biotechnology, and Biochemistry, Vol. 58, No. 12, 01.01.1994, p. 2244-2245.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Angiotensin I-converting Enzyme Inhibitory Peptides in an Alkaline Protease Hydrolyzate Derived from Sardine Muscle
AU - Matsufuji, Hiroshi
AU - Matsui, Toshiro
AU - Nakashima, Masatoshi
AU - Osajima, Yutaka
AU - Seki, Eiji
AU - Osajima, Katsuhiro
PY - 1994/1/1
Y1 - 1994/1/1
N2 - 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.
AB - 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.
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UR - http://www.scopus.com/inward/citedby.url?scp=0028712310&partnerID=8YFLogxK
U2 - 10.1271/bbb.58.2244
DO - 10.1271/bbb.58.2244
M3 - Article
VL - 58
SP - 2244
EP - 2245
JO - Bioscience, Biotechnology and Biochemistry
JF - Bioscience, Biotechnology and Biochemistry
SN - 0916-8451
IS - 12
ER -