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Literature summary for 3.4.15.1 extracted from

  • Mallikarjun Gouda, K.G.; Gowda, L.R.; Rao, A.G.; Prakash, V.
    Angiotensin I-converting enzyme inhibitory peptide derived from glycinin, the 11S globulin of soybean (Glycine max) (2006), J. Agric. Food Chem., 54, 4568-4573.
    View publication on PubMed
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Application

Application Comment Organism
medicine the peptide Val-Leu-Ile-Val-Pro is resistant to digestion by proteases of the gastrointestinal tract. The antihypertensive property of this peptide derived from glycinin might find importance in the development of therapeutic functional foods Sus scrofa

Inhibitors

Inhibitors Comment Organism Structure
glycinin hydrolysate
-
 Sus scrofa
Val-Leu-Ile-Val-Pro IC50: 0.00169 mM. The peptide is resistant to digestion by proteases of the gastrointestinal tract. The antihypertensive property of this peptide derived from glycinin might find importance in the development of therapeutic functional foods Sus scrofa

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
kidney
-
 Sus scrofa
-
lung
-
 Sus scrofa
-

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.0045
-
 Val-Leu-Ile-Val-Pro
-
 Sus scrofa

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.00169
-
 IC50: 0.00169 mM. The peptide is resistant to digestion by proteases of the gastrointestinal tract. The antihypertensive property of this peptide derived from glycinin might find importance in the development of therapeutic functional foods Sus scrofa Val-Leu-Ile-Val-Pro