1996
DOI: 10.1515/bchm3.1996.377.4.259
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Short Communication

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, wi… Show more

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Cited by 69 publications
(1 citation statement)
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References 24 publications
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“…Thus, α s1 -CN-derived peptides RY, RYL, RYLG, YLGY and FYPEL exert both ACE-inhibitory and antioxidant activities [ 23 , 24 , 25 , 26 , 27 ]. ACE-inhibitory and opioid activities are exerted by sequences YGFLP [ 28 ] and YGFL [ 29 , 30 ]. Four of the analyzed peptides (RYLGY, LGY, YPFPGPI, and YLLF) have been reported to exert three or more activities.…”
Section: Resultsmentioning
confidence: 99%
“…Thus, α s1 -CN-derived peptides RY, RYL, RYLG, YLGY and FYPEL exert both ACE-inhibitory and antioxidant activities [ 23 , 24 , 25 , 26 , 27 ]. ACE-inhibitory and opioid activities are exerted by sequences YGFLP [ 28 ] and YGFL [ 29 , 30 ]. Four of the analyzed peptides (RYLGY, LGY, YPFPGPI, and YLLF) have been reported to exert three or more activities.…”
Section: Resultsmentioning
confidence: 99%