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

Rabi Simantov, Solomon H. Snyder

Research output: Contribution to journalArticle


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 HTyrGlyGlyPheLeuOH (Leucine-enkephalin) and HTyrGlyGlyPheMetOH (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.

Original languageEnglish (US)
Pages (from-to)781-788
Number of pages8
JournalLife Sciences
Issue number8
StatePublished - Apr 15 1976

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Pharmacology, Toxicology and Pharmaceutics(all)

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