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  • Title: Angiotensin-I-converting enzyme inhibitory peptides from tryptic hydrolysate of bovine alphaS2-casein.
    Author: Tauzin J, Miclo L, Gaillard JL.
    Journal: FEBS Lett; 2002 Nov 06; 531(2):369-74. PubMed ID: 12417344.
    Abstract:
    Angiotensin-I-converting enzyme (ACE) inhibitory activity of a tryptic digest of bovine alpha(S2)-casein (alpha(S2)-CN) was extensively investigated. Forty-three peptide peaks were isolated and tested. Seven casokinins (i.e. CN-derived ACE inhibitory peptides) were identified and their IC50 values were determined. Four peptides exhibited an IC50 value lower than 20 microM. Peptides alpha(S2)-CN (f174-181) and alpha(S2)-CN (f174-179) had IC50 values of 4 microM. Surprisingly, deletion of the C-terminal dipeptide of two of these casokinins did not significantly alter their inhibitory activity.
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