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Isolation and structure identification of a morphine-like peptide “enkephalin” in bovine brain

Authors
Journal
Life Sciences
0024-3205
Publisher
Elsevier
Publication Date
Volume
18
Issue
8
Identifiers
DOI: 10.1016/0024-3205(76)90002-3

Abstract

Abstract The ability of bovine brain extracts to compete in a selective fashion for opiate receptor binding is attributable to a small peptide. The substance has been purified to homogeneity and identified as comprising two penta-peptides HTyrGlyGlyPheLeuOH (Leucine-enkephalin) and HTyrGlyGlyPheMetOH (methionine enkephalin). Bovine brain contains 4 times as much leucine-enkephalin as methionine-enkephalin in contrast to pig brain in which these ratios are reversed. Competition for opiate receptor binding by leucine-enkephalin is reduced more by sodium and enhanced more by manganese than is the case for methionine-enkephalin, suggesting that leucine-enkephalin may be a “purer” agonist than methionine-enkephalin.

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