Synthetic peptides corresponding to alpha-lactalbumin and beta-lactoglobulin sequences with angiotensin-I-converting enzyme inhibitory activity.

Biological chemistry Hoppe-Seyler Pub Date : 1996-04-01 DOI:10.1515/bchm3.1996.377.4.259
M M Mullally, H Meisel, R J FitzGerald
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引用次数: 168

Abstract

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.

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合成具有抑制血管紧张素- i转换酶活性的α -乳白蛋白和β -乳球蛋白序列对应的肽。
在已知具有阿片活性的β -乳球蛋白和α -乳白蛋白序列对应的合成肽中检测到新的血管紧张素- i转换酶(ACE)抑制活性。以hippuryl-histidyl-leucine为底物，四肽β -乳啡肽(Tyr-Leu-Leu-Phe)、α -乳啡肽(Tyr-Gly-Leu-Phe)和β -乳绷素(His-Ile-Arg-Leu)的IC50值分别为171.8、733.3和1153.2微米。相关二肽也能抑制ACE，其中Tyr-Leu的抑制作用最强，IC50值为122.1微米。
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Biological chemistry Hoppe-Seyler
Biological chemistry Hoppe-Seyler
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