Premium
Angiotensin‐I‐converting enzyme inhibitory peptides from tryptic hydrolysate of bovine α S2 ‐casein
Author(s) -
Tauzin Jérôme,
Miclo Laurent,
Gaillard Jean-Luc
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)03576-7
Subject(s) - ic50 , hydrolysate , chemistry , peptide , casein , dipeptide , enzyme , renin–angiotensin system , alpha (finance) , angiotensin converting enzyme , biochemistry , inhibitory postsynaptic potential , in vitro , endocrinology , hydrolysis , biology , medicine , construct validity , nursing , patient satisfaction , blood pressure
Angiotensin‐I‐converting enzyme (ACE) inhibitory activity of a tryptic digest of bovine α S2 ‐casein (α 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 IC 50 values were determined. Four peptides exhibited an IC 50 value lower than 20 μM. Peptides α S2 ‐CN (f174–181) and α S2 ‐CN (f174–179) had IC 50 values of 4 μM. Surprisingly, deletion of the C‐terminal dipeptide of two of these casokinins did not significantly alter their inhibitory activity.