[Endorphins, hypothalamic and neurohypophysial peptides with morphinomimetic activity: isolation and molecular structure of alpha-endorphin].
From a crude extract of Porcine neurohypophysis-hypothalamus we have isolated several peptides called endorphins which mimic opiated in a classical bioassay for morphine. Similarly they bind to the stereospecific synaptosomal opiates receptors of Rat brain in competition to 3 H-etorphine. The primary structure of alpha-endorphin is H-Tyr-Gly-Gly-Phe-Met-Thr-Ser-Glu-Lys-Ser-Gln-Thr-Pro-Leu-Val-Thr-OH. Met-enkephalin is the N-terminal pentapeptide of alpha-endorphin. Alpha-endorphin has the same sequence as that of the fragment TYR 61 to Thr 76 of the beta-lipotropins.
D000595:Amino Acid Sequence; D000818:Animals; D001681:Biological Assay; D002417:Cattle; D007031:Hypothalamus / Q000032:analysis*; D009020:Morphine / Q000378:metabolism; D009419:Nerve Tissue Proteins / Q000032:analysis* / Q000302:isolation & purification; D010455:Peptides / Q000032:analysis* / Q000138:chemical synthesis / Q000302:isolation & purification; D010904:Pituitary Gland, Posterior / Q000032:analysis*; D051381:Rats; D011955:Receptors, Drug; D013552:Swine
D009419:Nerve Tissue Proteins; D010455:Peptides; D011955:Receptors, Drug; D009020:Morphine
Endorphines, peptides, d'origine hypothalamique et neurohypophysaire à activité morphinomimétique. Isolement et structure moléculaire de l'alpha-endorphine