Tandem multimer expression of angiotensin I-converting enzyme inhibitory peptide in Escherichia coli

2009 ◽  
Vol 4 (9) ◽  
pp. 1345-1356 ◽  
Author(s):  
Hasan M. Fida ◽  
Yoichi Kumada ◽  
Masaaki Terashima ◽  
Tomohisa Katsuda ◽  
Shigeo Katoh
Keyword(s):  
Escherichia Coli ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Inhibitory Peptide ◽  
Angiotensin I Converting Enzyme

scholarly journals Separation and Purification of Angiotensin I Converting Enzyme Inhibitory Peptide in Peptic Hydrolyzate of Oyster.

1994 ◽  
Vol 41 (9) ◽  
pp. 589-594 ◽  
Author(s):  
Kiyoshi MATSUMOTO ◽  
Atsuko OGIKUBO ◽  
Takatada YOSHINO ◽  
Toshiro MATSUI ◽  
Yutaka OSAJIMA
Keyword(s):  
Converting Enzyme ◽  
Separation And Purification ◽  
Angiotensin I ◽  
Inhibitory Peptide ◽  
Angiotensin I Converting Enzyme

Evaluation and Identification of Potent Angiotensin-I Converting Enzyme Inhibitory Peptide Derived from Dwarf Gulper Shark (C entrophorus atromarginatus )

2014 ◽  
Vol 39 (2) ◽  
pp. 107-115 ◽  
Author(s):  
Asami Ikeda ◽  
Hayato Ichino ◽  
Saori Kiguchiya ◽  
Petros Chigwechokha ◽  
Masaharu Komatsu ◽  
...  
Keyword(s):  
Converting Enzyme ◽  
Angiotensin I ◽  
Inhibitory Peptide ◽  
Angiotensin I Converting Enzyme

Inhibitory mechanism of a substrate-type angiotensin I-converting enzyme inhibitory peptide

2019 ◽  
Vol 79 ◽  
pp. 97-104 ◽  
Author(s):  
Junjie Wu ◽  
Dewei Xie ◽  
Xujun Chen ◽  
Ya-Jie Tang ◽  
Lixin Wang ◽  
...  
Keyword(s):  
Converting Enzyme ◽  
Inhibitory Mechanism ◽  
Substrate Type ◽  
Angiotensin I ◽  
Inhibitory Peptide ◽  
Angiotensin I Converting Enzyme

Novel angiotensin-I-converting enzyme inhibitory peptides derived from recombinant human αs1-casein expressed in Escherichia coli

1999 ◽  
Vol 66 (3) ◽  
pp. 431-439 ◽  
Author(s):  
YOO-KYEONG KIM ◽  
SUN YOON ◽  
DAE-YEUL YU ◽  
BO LÖNNERDAL ◽  
BONG-HYUN CHUNG
Keyword(s):  
Escherichia Coli ◽  
Amino Acid Sequences ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Ace Inhibitory Activity ◽  
Inhibitory Peptides ◽  
Angiotensin I Converting Enzyme ◽  
Ace Inhibitory Peptides ◽  
Treatment Of Hypertension ◽  
Ace Inhibitory

Recombinant human αs1-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.

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