Dehydro-enkephalins [ΔAla2]-, [ΔAla3]-, [ΔPhe4]-, and [ΔLeu5]enkephalins, were examined for their stability to enzymatic hydrolysis by carboxypeptidase Y [EC 126.96.36.199]. The successively liberated amino acids were determined quantitatively by amino acid analyses. The saturated leucine-enkephalin was rapidly hydrolyzed from the COOH-terminus. However, peptide linkages with α,β-dehydroamino acid residues placed in the enkephalin molecule were strongly resistant to the enzyme at the carboxyl side and completely resistant at the amino side of the dehydro residue. © 1982.
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