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PMID: 1069261 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Isolation, primary structure, and synthesis of alpha-endorphin and gamma-endorphin, two peptides of hypothalamic-hypophysial origin with morphinomimetic activity.

Ling N, Burgus R, Guillemin R

Abstract

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.

MeSH Terms
Amino Acid Sequence Animals Hypothalamus/chemistry Nerve Tissue Proteins/analysis,chemical synthesis Peptides/analysis,chemical synthesis Pituitary Gland, Posterior/chemistry Swine
Chemicals
Nerve Tissue Proteins Peptides
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Ling N
Burgus R
Guillemin R
References (19)
19 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1976-11-00
Pages
3942-6
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC431275
Subset
IM
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