Isolation, primary structure, and synthesis of alpha-endorphin and gamma-endorphin, two peptides of hypothalamic-hypophysial origin with morphinomimetic activity.
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 alpha-endorphin and gamma-endophin, was determined by mass spectrometry and danxyl-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 beta-lipotropins. A third peptide also obtained in pure form in these studies was found to be an unstable salt of alpha-endorphin.
D000595:Amino Acid Sequence; D000818:Animals; D007031:Hypothalamus / Q000737:chemistry*; D009419:Nerve Tissue Proteins / Q000032:analysis / Q000138:chemical synthesis; D010455:Peptides / Q000032:analysis / Q000138:chemical synthesis; D010904:Pituitary Gland, Posterior / Q000737:chemistry*; D013552:Swine
D009419:Nerve Tissue Proteins; D010455:Peptides