SYNTHETIC PEPTIDES CORRESPONDING TO ALPHA-LACTALBUMIN AND BETA-LACTOGLOBULIN SEQUENCES WITH ANGIOTENSIN-I-CONVERTING ENZYME-INHIBITORY ACTIVITY

Authors
MULLALLY MM MEISEL H FITZGERALD RJ
Citation
Mm. Mullally et al., SYNTHETIC PEPTIDES CORRESPONDING TO ALPHA-LACTALBUMIN AND BETA-LACTOGLOBULIN SEQUENCES WITH ANGIOTENSIN-I-CONVERTING ENZYME-INHIBITORY ACTIVITY, Biological chemistry Hoppe-Seyler, 377(4), 1996, pp. 259-260
Citations number
12
Categorie Soggetti
Biology
Journal title
Biological chemistry Hoppe-Seyler → ACNP
ISSN journal
01773593
Volume
377
Issue
4
Year of publication
1996
Pages
259 - 260
Database
ISI
SICI code
0177-3593(1996)377:4<259:SPCTAA>2.0.ZU;2-O
Abstract
Novel angiotensin-I-converting enzyme (ACE) inhibitory activities were detected in synthetic peptides corresponding to sequences of beta-lac toglobulin and alpha-lactalbumin and which are known to possess opioid activity. Using hippuryl-histidyl-leucine as substrate, the tetrapept ides beta-lactorphin (Tyr-Leu-Leu-Phe), alpha-lactorphin (Tyr-Gly-Leu- Phe) and beta-lactotensin (His-Ile-Arg-Leu) were shown to have IC50 va lues of 171.8, 733.3 and 1153.2 mu M, respectively. Related dipeptides also inhibited ACE, with Tyr-Leu being the most potent, having an IC5 0 value of 122.1 mu M.