The enzyme stability of dehydro-enkephalins

  • Shimohigashi Y
  • Chen H
  • Stammer C
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Dehydro-enkephalins [ΔAla2]-, [ΔAla3]-, [ΔPhe4]-, and [ΔLeu5]enkephalins, were examined for their stability to enzymatic hydrolysis by carboxypeptidase Y [EC]. 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.

Author-supplied keywords

  • Carboxypeptidase
  • Dehydro-enkephalin
  • Enkephalin
  • Enzyme stability

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  • Yasuyuki Shimohigashi

  • Hao Chia Chen

  • Charles H. Stammer

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