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29 March 2024 |
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Isolation and structure of a novel C-terminally amidated opioid peptide, amidorphin, from bovine adrenal medulla | B R Seizinger
; D C Liebisch
; C Gramsch
; A Herz
; E Weber
; C J Evans
; F S Esch
; P Böhlen
; | Date: |
3 Jan 1985 | Journal: | Nature, 313 (5997), 57-9 | Abstract: | Biologically active peptide hormones and neurotransmitters have been shown to be enzymatically liberated from larger, inactive precursor molecules by tissue-specific post-translational processing, particularly at the typical cleavage signals of paired basic residues. Subsequent N-terminal or C-terminal modifications may be of importance in regulating the biological activities of these peptides. C-terminal alpha-amidation is considered to be essential for the biological function of several non-opioid peptides. Here we present the isolation and structure of a novel C-terminally amidated opioid peptide, amidorphin, from bovine adrenal medulla. Amidorphin and the recently isolated octapeptide metorphamide (adrenorphin) are the only endogenous opioid peptides in mammals known to possess a C-terminal amide group. The amino acid sequence of amidorphin corresponds to the sequence 104-129 of bovine proenkephalin A. Very high concentrations of amidorphin were detected in bovine adrenal medulla and in a further endocrinological system, the hypothalamic-neurohypophyseal axis. Amidorphin may therefore be considered to be a major gene product of the opioid peptide precursor proenkephalin A in these endocrine tissues. | Source: | PubMed, pmid3965972 | Services: | Forum | Review | Favorites |
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