Literature DB >> 8737991

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

M M Mullally1, H Meisel, R J FitzGerald.   

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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Year:  1996        PMID： 8737991     DOI： 10.1515/bchm3.1996.377.4.259

Source DB:  PubMed          Journal:  Biol Chem Hoppe Seyler        ISSN： 0177-3593


  7 in total

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  7 in total

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