TY - JOUR
T1 - Synthetic peptides corresponding to α-lactalbumin and β-lactoglobulin sequences with angiotensin-i-converting enzyme inhibitory activity
AU - Mullally, Margaret M.
AU - Meisel, Hans
AU - Fitzgerald, Richard J.
PY - 1996
Y1 - 1996
N2 - Novel angiotensin-l-converting enzyme (ACE) inhibitory activities were detected in synthetic peptides corresponding to sequences of β-lactoglobulin and α-lactalbumin and which are known to possess opioid activity. Using hippuryl-histidyl-leucine as substrate, the tetrapeptides β-lactorphin (Tyr-Leu-Leu-Phe), alactorphin (Tyr-Gly-Leu-Phe) and β-lactotensin (HisIle-Arg-Leu) were shown to have ICso values of 171.8, 733.3 and 1153.2 JAM, respectively. Related dipeptides also inhibited ACE, with Tyr-Leu being the most potent, having an ICso value of 122.1 \M.
AB - Novel angiotensin-l-converting enzyme (ACE) inhibitory activities were detected in synthetic peptides corresponding to sequences of β-lactoglobulin and α-lactalbumin and which are known to possess opioid activity. Using hippuryl-histidyl-leucine as substrate, the tetrapeptides β-lactorphin (Tyr-Leu-Leu-Phe), alactorphin (Tyr-Gly-Leu-Phe) and β-lactotensin (HisIle-Arg-Leu) were shown to have ICso values of 171.8, 733.3 and 1153.2 JAM, respectively. Related dipeptides also inhibited ACE, with Tyr-Leu being the most potent, having an ICso value of 122.1 \M.
KW - IC50
KW - Multifunctional bioactivity
KW - Nutraceutical
KW - Opioid peptides
UR - http://www.scopus.com/inward/record.url?scp=0029937138&partnerID=8YFLogxK
M3 - Article
C2 - 8737991
AN - SCOPUS:0029937138
SN - 0177-3593
VL - 377
SP - 259
EP - 260
JO - Biological Chemistry Hoppe-Seyler
JF - Biological Chemistry Hoppe-Seyler
IS - 4
ER -