In vitro quantitative study of the degradation of endomorphins

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Abstract

The catabolism of the endomorphins was investigated in detail. The endomorphins were degraded relatively slowly in the rat brain homogenate (t1/2(endomorphin-1)=4.94min; t1/2(endomorphin-2)=3.81min). The inhibition of metalloproteases and aminopeptidases stabilised the endomorphins to the greatest extent. The digestion of endomorphins tritiated specifically on Tyr1, Pro2 or Phe3 established also that only the aminopeptidase pathways were essential for inactivation of the endomorphins, and that the tetrapeptides were degraded by cleavage of the Pro2-Trp3 or Pro2-Phe3 bond. The end-products of the catabolism were amino acids; the fragments Tyr-Pro-OH and Pro-Trp-Phe-NH2 were present as intermediates. Metabolites produced by brain carboxypeptidases were not detected.

Original languageEnglish
Pages (from-to)1573-1580
Number of pages8
JournalPeptides
Volume23
Issue number9
DOIs
Publication statusPublished - Sep 1 2002

Keywords

  • Endomorphin
  • HPLC
  • Half-life
  • Metabolism
  • Opioid
  • Peptide
  • Tritium

ASJC Scopus subject areas

  • Biochemistry
  • Physiology
  • Endocrinology
  • Cellular and Molecular Neuroscience

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