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与具有血管紧张素-I转换酶抑制活性的α-乳白蛋白和β-乳球蛋白序列相对应的合成肽。

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

作者信息

Mullally M M, Meisel H, FitzGerald R J

机构信息

National Dairy Products Research Centre, Fermoy, Co. Cork, Ireland.

出版信息

Biol Chem Hoppe Seyler. 1996 Apr;377(4):259-60. doi: 10.1515/bchm3.1996.377.4.259.

DOI:10.1515/bchm3.1996.377.4.259
PMID:8737991
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.

摘要

在与β-乳球蛋白和α-乳白蛋白序列相对应且已知具有阿片样物质活性的合成肽中检测到了新型血管紧张素转换酶（ACE）抑制活性。以马尿酰-组氨酰-亮氨酸为底物，四肽β-乳啡肽（酪氨酸-亮氨酸-亮氨酸-苯丙氨酸）、α-乳啡肽（酪氨酸-甘氨酸-亮氨酸-苯丙氨酸）和β-乳紧张素（组氨酸-异亮氨酸-精氨酸-亮氨酸）的IC50值分别为171.8、733.3和1153.2微摩尔。相关的二肽也抑制ACE，其中酪氨酸-亮氨酸最有效，IC50值为122.1微摩尔。

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