Hydrolysis of various bioactive peptides by goat brain dipeptidylpeptidase‐III homologue

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Abstract
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 (TyrGlyGlyPheLeu) at the GlyGly bond producing TyrGly and GlyPheLeu 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 NH2‐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.

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