Abstract
Peptidic fractions which inhibit angiotensin I-converting enzyme (ACE) were separated from peptic digests of soybean by ion exchange chromatography and gel filtration. Further separation of the peptidic fractions by ODS HPLC afforded active peptides, the amino acid sequences of which were identified by Edman's procedure as: Ile-Ala (inhibitory against ACE with an IC50 of 153 μM), Tyr-Leu-Ala-Gly-Asn-Gln (14 μM), Phe-Phe-Leu (37 μM), Ile-Tyr-Leu-Leu (42 μM), and Val-Met-Asp-Lys-Pro-Gln-Gly (39 μM). The antihypertensive activity of the soybean peptides was also investigated. Peptide fractions (2.0 g/kg body weight, oral administration) markedly lowered the blood pressure of spontaneously hypertensive rats (SHRs).
| Original language | English |
|---|---|
| Pages (from-to) | 543-554 |
| Number of pages | 12 |
| Journal | Journal of Food Biochemistry |
| Volume | 26 |
| Issue number | 6 |
| Publication status | Published - Dec 2002 |
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ASJC Scopus subject areas
- Food Science
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
Cite this
Identification of angiotensin I-converting enzyme inhibitory peptides derived from the peptic digest of soybean protein. / Chen, Jiun-Rong; Okada, Takashi; Muramoto, Koji; Suetsuna, Kunio; Yang, Suh-Ching.
In: Journal of Food Biochemistry, Vol. 26, No. 6, 12.2002, p. 543-554.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Identification of angiotensin I-converting enzyme inhibitory peptides derived from the peptic digest of soybean protein
AU - Chen, Jiun-Rong
AU - Okada, Takashi
AU - Muramoto, Koji
AU - Suetsuna, Kunio
AU - Yang, Suh-Ching
PY - 2002/12
Y1 - 2002/12
N2 - Peptidic fractions which inhibit angiotensin I-converting enzyme (ACE) were separated from peptic digests of soybean by ion exchange chromatography and gel filtration. Further separation of the peptidic fractions by ODS HPLC afforded active peptides, the amino acid sequences of which were identified by Edman's procedure as: Ile-Ala (inhibitory against ACE with an IC50 of 153 μM), Tyr-Leu-Ala-Gly-Asn-Gln (14 μM), Phe-Phe-Leu (37 μM), Ile-Tyr-Leu-Leu (42 μM), and Val-Met-Asp-Lys-Pro-Gln-Gly (39 μM). The antihypertensive activity of the soybean peptides was also investigated. Peptide fractions (2.0 g/kg body weight, oral administration) markedly lowered the blood pressure of spontaneously hypertensive rats (SHRs).
AB - Peptidic fractions which inhibit angiotensin I-converting enzyme (ACE) were separated from peptic digests of soybean by ion exchange chromatography and gel filtration. Further separation of the peptidic fractions by ODS HPLC afforded active peptides, the amino acid sequences of which were identified by Edman's procedure as: Ile-Ala (inhibitory against ACE with an IC50 of 153 μM), Tyr-Leu-Ala-Gly-Asn-Gln (14 μM), Phe-Phe-Leu (37 μM), Ile-Tyr-Leu-Leu (42 μM), and Val-Met-Asp-Lys-Pro-Gln-Gly (39 μM). The antihypertensive activity of the soybean peptides was also investigated. Peptide fractions (2.0 g/kg body weight, oral administration) markedly lowered the blood pressure of spontaneously hypertensive rats (SHRs).
UR - http://www.scopus.com/inward/record.url?scp=0037002214&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0037002214&partnerID=8YFLogxK
M3 - Article
AN - SCOPUS:0037002214
VL - 26
SP - 543
EP - 554
JO - Journal of Food Biochemistry
JF - Journal of Food Biochemistry
SN - 0145-8884
IS - 6
ER -