Physiologically Active Peptide Motif in Proteins : Peptide Inhibitors of ACE from the Hydrolysates of Antarctic Krill Muscle Protein
Japan Agricultural Research Quarterly
ISSN | 00213551 |
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NII recode ID (NCID) | AA0068709X |
Full text
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A peptide which inhibits the angiotensin-converting enzyme (ACE) was separated from sequential hydrolysates of defatted Antarctic krill muscle by pepsin and trypsin. The preparation procedure included chromatography on SP-Sephadex C-25, Superose 12, and reverse phase HPLC. The peptide fraction with the ACE-inhibiting activity was nearly pure and the main component was found to be a peptide with the amino acid sequence of Lys-Leu-Lys-Phe-Val showing a half-maximum inhibition concentration (1C50) of 30 μmol/l. A peptide sequence with 66% homology to the present peptide was found in some proteins such as prostaglandin DII reductase, thrombospondin precursor, epidermal growth factor precursor.
Date of issued | |
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Creator | Yukio KAWAMURA Toshikazu TAKANE Mikio SATAKE Toshio SUGIMOTO |
Available Online | |
NII resource type vocabulary | Journal Article |
Volume | 26 |
Issue | 3 |
spage | 210 |
epage | 213 |
Language | eng |