Abstract
We report here the isolation of α-glucosidase (AGH) inhibitory peptides derived from sardine muscle hydrolyzate, which was prepared by digestion with Bacillus licheniformis alkaline protease. As a result of reversed-phase HPLC purification, two AGH inhibitory peptides were isolated from a DEAE-Sephadex A-25 column eluate. The peptides were identified as follows: Val-Trp (IC50 = 22.6 mM) and Try-Tyr-Pro-Leu (IC50 ± 3.7 mM). AGH inhibitory studies of Try-Tyr-Pro-Leu and its derivatives demonstrated the importance of the tripeptide chain length as well as the hydrophobic aromatic amino acid tyrosine at the N-terminus, aliphatic amino acids at the C-terminus, as well as an amide proton from the peptide chain at the middle position of the tri-peptide to develop AGH inhibition activity.
| Original language | English |
|---|---|
| Pages (from-to) | 259-263 |
| Number of pages | 5 |
| Journal | Zeitschrift fur Naturforschung - Section C Journal of Biosciences |
| Volume | 54 |
| Issue number | 3-4 |
| DOIs | |
| Publication status | Published - Jan 1 1999 |
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All Science Journal Classification (ASJC) codes
- Biochemistry, Genetics and Molecular Biology(all)
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Isolation and identification of peptidic α-glucosidase inhibitors derived from sardine muscle hydrolyzate. / Matsui, Toshiro; Oki, Tomoyuki; Osajima, Yutaka.
In: Zeitschrift fur Naturforschung - Section C Journal of Biosciences, Vol. 54, No. 3-4, 01.01.1999, p. 259-263.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Isolation and identification of peptidic α-glucosidase inhibitors derived from sardine muscle hydrolyzate
AU - Matsui, Toshiro
AU - Oki, Tomoyuki
AU - Osajima, Yutaka
PY - 1999/1/1
Y1 - 1999/1/1
N2 - We report here the isolation of α-glucosidase (AGH) inhibitory peptides derived from sardine muscle hydrolyzate, which was prepared by digestion with Bacillus licheniformis alkaline protease. As a result of reversed-phase HPLC purification, two AGH inhibitory peptides were isolated from a DEAE-Sephadex A-25 column eluate. The peptides were identified as follows: Val-Trp (IC50 = 22.6 mM) and Try-Tyr-Pro-Leu (IC50 ± 3.7 mM). AGH inhibitory studies of Try-Tyr-Pro-Leu and its derivatives demonstrated the importance of the tripeptide chain length as well as the hydrophobic aromatic amino acid tyrosine at the N-terminus, aliphatic amino acids at the C-terminus, as well as an amide proton from the peptide chain at the middle position of the tri-peptide to develop AGH inhibition activity.
AB - We report here the isolation of α-glucosidase (AGH) inhibitory peptides derived from sardine muscle hydrolyzate, which was prepared by digestion with Bacillus licheniformis alkaline protease. As a result of reversed-phase HPLC purification, two AGH inhibitory peptides were isolated from a DEAE-Sephadex A-25 column eluate. The peptides were identified as follows: Val-Trp (IC50 = 22.6 mM) and Try-Tyr-Pro-Leu (IC50 ± 3.7 mM). AGH inhibitory studies of Try-Tyr-Pro-Leu and its derivatives demonstrated the importance of the tripeptide chain length as well as the hydrophobic aromatic amino acid tyrosine at the N-terminus, aliphatic amino acids at the C-terminus, as well as an amide proton from the peptide chain at the middle position of the tri-peptide to develop AGH inhibition activity.
UR - http://www.scopus.com/inward/record.url?scp=0033103875&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0033103875&partnerID=8YFLogxK
U2 - 10.1515/znc-1999-3-417
DO - 10.1515/znc-1999-3-417
M3 - Article
C2 - 10408829
AN - SCOPUS:0033103875
VL - 54
SP - 259
EP - 263
JO - Zeitschrift fur Naturforschung - Section C Journal of Biosciences
JF - Zeitschrift fur Naturforschung - Section C Journal of Biosciences
SN - 0939-5075
IS - 3-4
ER -