Short Communication

作者：Margaret M. Mullally, Hans-Joerg Meisel, Richard J. Fitzgerald · 发表于：Biological Chemistry Hoppe-Seyler · 年份：1996 · DOI：10.1515/bchm3.1996.377.4.259 · 被引用次数：152 · 研究领域：Protein Hydrolysis and Bioactive Peptides、Neuropeptides and Animal Physiology、Peptidase Inhibition and Analysis

Novel angiotensin-I-converting enzyme (ACE) inhibitory activities were detected in synthetic peptides corresponding to sequences of beta-lactoglobulin and alpha-lactalbumin and which are known to possess opioid activity. Using hippuryl-histidyl-leucine as substrate, the tetrapeptides beta-lactorphin (Tyr-Leu-Leu-Phe), alpha-lactorphin (Tyr-Gly-Leu-Phe) and beta-lactotensin (His-Ile-Arg-Leu) were shown to have IC50 values of 171.8, 733.3 and 1153.2 microM, respectively. Related dipeptides also inhibited ACE, with Tyr-Leu being the most potent, having an IC50 value of 122.1 microM.