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Formation of [Leu 5 ]Enkephalin from Dynorphin A(1–8) by Rat Central Nervous Tissue In Vitro
Author(s) -
Dixon D. M.,
Traynor J. R.
Publication year - 1990
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1990.tb01972.x
Subject(s) - dynorphin , leu enkephalin , enkephalin , chemistry , dynorphin a , thiorphan , proenkephalin , biochemistry , central nervous system , oligopeptidase , in vitro , endopeptidase , enzyme , medicine , endocrinology , opioid peptide , enzyme inhibitor , biology , opioid , receptor
[ 3 H]Dynorphin A(1–8) is readily metabolised by rat lumbosacral spinal cord tissue in vitro, affording a variety of products including a significant amount (20% recovered activity) of [ 3 H][Leu 5 ]enkephalin. In the presence of the peptidase inhibitors bestatin, captopril, thiorphan, and leucylleucine, [ 3 H][Leu 5 ]enkephalin was the major metabolic product, accounting for 60% of recovered activity. Production of [ 3 H][Leu 5 ]enkephalin was seen across all gross brain regions. The enzyme responsible for the cleavage has an optimal substrate length of 8–13 amino acids and is inhibited b N ‐[1‐( RS )‐carboxy‐2‐phenylethyl]‐Ala‐Ala‐Phe‐ p ‐aminobenzoate, a site‐directed inhibitor of the metalloendopeptidase EC 3.4.24.15. However the enzymic breakdown also has properties in common with involvement of endo‐oligopeptidase A. Possible consequences of the formation of [Leu 5 ]enkephalin from the smaller dynorphins are discussed.