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Angiotensin I-converting enzyme inhibitory oligo-tyrosine peptides synthesized by α-chymotrypsin

Paper ID Volume ID Publish Year Pages File Format Full-Text
17600 42682 2009 7 PDF Available
Title
Angiotensin I-converting enzyme inhibitory oligo-tyrosine peptides synthesized by α-chymotrypsin
Abstract

Oligo-tyrosine peptides with degrees of polymerization ranging from 2 to 5 could be synthesized by α-chymotrypsin-catalyzed reaction with l-tyrosine ethyl ester in aqueous media, although the peptide yield was low due to a preferential hydrolysis of the substrate. It was also confirmed that α-chymotrypsin efficiently converted tyrosine tetramer to the dimer which was resistant to the digestion. Both Tyr-Tyr and Tyr-Tyr-Tyr showed high inhibitory activity for angiotensin I-converting enzyme from rabbit lung, and their IC50 values were 34 μM and 51 μM, respectively. These two peptides exhibited a mix of competitive and noncompetitive inhibitions. Tyr-Tyr-Tyr was first recognized as an ACE inhibitor, suggesting that α-chymotrypsin could be applied to synthesis of novel potential materials for antihypertensive medicines.

Keywords
ACE, angiotensin I-converting enzyme; CPase Y, carboxypeptidase Y; DHBA, 2,5-dihydroxybenzoic acid; DP, degree of polymerization; HA, hippuric acid; HHL, hippuryl histidyl leucine; MALDI-TOFMS, matrix-assisted laser desorption/ionization time of flight ma
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Angiotensin I-converting enzyme inhibitory oligo-tyrosine peptides synthesized by α-chymotrypsin
Publisher
Database: Elsevier - ScienceDirect
Journal: Enzyme and Microbial Technology - Volume 44, Issue 4, 6 April 2009, Pages 235–241
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering