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The isolation and primary structure of two peptides with morphinomimetic activity, obtained from an extract of porcine hypothalamus-neurohypophysis, are described. The amino acid sequence of the two peptides, named α-endorphin and γ-endorphin, was determined by mass spectrometry and densyl-Edman methods to be H-Tyr-Gly-Gly-Phe-Met-Thr-Ser-Glu-Lys-Ser-Gln-Thr-Pro-Leu-Val-Thr-OH and H-Tyr-Gly-Gly-Phe-Met-Thr-Ser-Glu-Lys-Ser-Gln-Thr-Pro-Leu-Val-Thr-Leu-OH, respectively. These correspond to the amino acid sequences present between residues 61 and 76 and residues 61 and 77 of the various β-lipotropins. A third peptide also obtained in pure from in these studies was found to be an unstable salt of α-endorphin.

proceedings of the national academy of sciences of the united states of america

Isolation, primary structure, and synthesis of α-endorphin and γ-endorphin, two peptides of hypothalamic-hypophysial origin with morphinomimetic activity