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Title 

Novel agiotensin-I-converting enzyme inhibitory peptides derived from recombinant human alphas1-casein expressed in Escherichia coli

Authors 

Yoo Kyeong KimSun YoonDae Yeul YuBo LonnerdalBong Hyun Chung

Publisher 

Cambridge University Press (CUP)

Issue Date 

1999

Citation 

Journal of Dairy Research, vol. 66, no. 0, pp. 431-439

Keywords 

peptide fragmentsrecombinant proteins

Abstract 

Recombinant human α(s1)-casein expressed in Escherichia coli was purified and digested with trypsin in an attempt to find peptides with angiotensin-I-converting enzyme (ACE) inhibitory activity. Three novel ACE inhibitory peptides, A-II. B-II and C, were isolated and their amino acid sequences identified as Tyr-Pro-Glu-Arg (residues 8-11), Tyr-Tyr-Pro-Gln-Ile-Met-Gln-Tyr (residues 136-143) and Asn-Asn-Val-Met-Leu-Gln-Trp (residues 164-170) respectively. ACE inhibitory activities were measured for the corresponding synthetic peptides, and the ACE IC50 (the amount of peptide causing 50% inhibition of ACE activity) values of A-II, B-II and C estimated to be 132.5, 24.8 and 41.0 μmol/l respectively. Peptides A-II and C were resistant to further digestion by pepsin, whereas peptide B-II was hydrolysed. All three peptides were resistant to digestion by chymotrypsin. These ACE inhibitory peptides may prove useful for oral administration in the treatment of hypertension.

ISSN 

0022-0299

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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