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Hydrolysis of various bioactive peptides by goat brain dipeptidylpeptidase‐III homologue
Author(s) -
Dhanda Suman,
Singh Jasbir,
Singh Hari
Publication year - 2008
Publication title -
cell biochemistry and function
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.933
H-Index - 61
eISSN - 1099-0844
pISSN - 0263-6484
DOI - 10.1002/cbf.1448
Subject(s) - tetrapeptide , chemistry , hydrolysis , tripeptide , enkephalin , biochemistry , enzyme , dipeptidyl peptidase , oligopeptide , moiety , renin–angiotensin system , peptide , hydrolysate , angiotensin iii , stereochemistry , angiotensin ii , endocrinology , biology , receptor , angiotensin ii receptor type 1 , opioid , blood pressure
DPP‐III from goat brain was purified to apparent electrophoretic homogeneity which showed several characteristics similar to other reported DPP‐IIIs although it possesses dissimilar molecular weight and different inhibition behavior. Thin layer chromatographic studies with goat brain DPP‐III revealed that it hydrolyses Leu‐enkephalin (TyrGlyGlyPheLeu) at the GlyGly bond producing TyrGly and GlyPheLeu with no further degradation of liberated tripeptide. (Ala) 4 is hydrolyzed to dialanine whereas trialanine is not cleaved. ACTH, angiotensin II and III were also hydrolyzed whereas angiotensin I was not. It was concluded that the enzyme requires at least a tetrapeptide to act and that it removes a dipeptidyl moiety from the NH 2 ‐terminus of the studied peptides. Goat brain DPP‐III may be involved in the metabolism of very important bioactive peptides such as enkephalins and angiotensins. Copyright © 2007 John Wiley & Sons, Ltd.