Physiologically active peptide motif in proteins: Peptide inhibitors of ACE from the hydrolysates of antarctic krill muscle protein
1992
Kawamura, Y. (National Food Research Inst., Tsukuba, Ibaraki (Japan)) | Takane, T. | Satake, M. | Sugimoto, T.
A peptide which inhibits the angiotensin-converting enzyme(ACE) was separated from sequential hydroysates 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 sequence of Lys-Leu-Lys-Phe-Val showing a half-maximum inhibition concentration (IC50) of 30 mumol/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
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