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International journal of peptide and protein research1981; 18(3); 242-248; doi: 10.1111/j.1399-3011.1981.tb02978.x

beta-Endorphin: isolation, amino acid sequence and synthesis of the hormone from horse pituitary glands.

Abstract: Beta-endorphin has been isolated from equine pituitaries. Its amino acid sequence is identical to that of ovine, bovine and camel beta-endorphins except for substitution of the threonine residue at position 6 by serine. The equine beta-endorphin has also been synthesized by the solid-phase method. In comparison with the human hormone, equine beta-endorphin was shown to possess 3 times the receptor-binding activity in rat membrane preparations and 1.6 times the analgesic potency in the mouse tail-flick assay.
Publication Date: 1981-09-01 PubMed ID: 6281204DOI: 10.1111/j.1399-3011.1981.tb02978.xGoogle Scholar: Lookup
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  • Journal Article
  • Research Support
  • Non-U.S. Gov't
  • Research Support
  • U.S. Gov't
  • P.H.S.

Summary

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This research isolates the hormone beta-endorphin from horse pituitary glands, determining that the structure is similar to the beta-endorphin found in sheep, cows, and camels. It’s found to have enhanced receptor-binding activity and analgesic potency compared to human beta-endorphin.

Extraction and Identification of Equine Beta-Endorphin

  • The researchers managed to isolate the hormone beta-endorphin specifically from equine (horse) pituitary glands. Once isolated, the structure of this beta-endorphin was examined to identify its unique amino acid sequence.
  • This sequence was found to be similar to those of beta-endorphin in ovine (sheep), bovine (cows), and camel species. The only difference was a substitution of the threonine residue (an amino acid type) at a specific position with another amino acid, serine. This shows a significant degree of evolutionary similarity between these species.

Synthesis of Equine Beta-Endorphin

  • The study also demonstrated the successful synthesis of equine beta-endorphin using the solid-phase method. Solid-phase synthesis is a commonly used method in biochemistry for producing peptides (chains of amino acids) in a controlled manner.

Comparison with Human Beta-Endorphin

  • Further, the study compared the properties of equine beta-endorphin to those of the human variant. This comparison revealed that horse beta-endorphin has three times greater receptor-binding activity in rat membrane preparations. This means that it has a stronger ability to bind to specific receptors in these cells, which can potentially initiate a biological response.
  • Moreover, the equine form of the hormone also demonstrated 1.6 times the analgesic (pain-relieving) potency in a standard experimental measure known as the mouse tail-flick assay. This implies that equine beta-endorphin could be more effective at reducing pain than the human version.

Implications of the Research

  • The findings suggest that equine beta-endorphin might be an interesting target for future research on new analgesic drugs due to its high potency.
  • Additionally, the successful synthesis of the equine hormone could facilitate further experimental studies and possibly pharmaceutical applications.

Cite This Article

APA
Li CH, Ng TB, Yamashiro D, Chung D, Hammonds RG, Tseng LF. (1981). beta-Endorphin: isolation, amino acid sequence and synthesis of the hormone from horse pituitary glands. Int J Pept Protein Res, 18(3), 242-248. https://doi.org/10.1111/j.1399-3011.1981.tb02978.x

Publication

ISSN: 0367-8377
NlmUniqueID: 0330420
Country: Denmark
Language: English
Volume: 18
Issue: 3
Pages: 242-248

Researcher Affiliations

Li, C H
    Ng, T B
      Yamashiro, D
        Chung, D
          Hammonds, R G
            Tseng, L F

              MeSH Terms

              • Amino Acid Sequence
              • Amino Acids / analysis
              • Analgesics
              • Animals
              • Chemical Phenomena
              • Chemistry
              • Chromatography
              • Endorphins / chemical synthesis
              • Endorphins / isolation & purification
              • Endorphins / pharmacology
              • Horses / metabolism
              • Pituitary Gland / analysis
              • Rats
              • Receptors, Opioid / metabolism
              • beta-Endorphin

              Grant Funding

              • GM-2907 / NIGMS NIH HHS
              • MH-30245 / NIMH NIH HHS

              Citations

              This article has been cited 3 times.
              1. Asvadi NH, Morgan M, Herath HM, Hewavitharana AK, Shaw PN, Cabot PJ. Beta-endorphin 1-31 biotransformation and cAMP modulation in inflammation. PLoS One 2014;9(3):e90380.
                doi: 10.1371/journal.pone.0090380pubmed: 24618600google scholar: lookup
              2. Nicolas P, Hammonds RG Jr, Li CH. Beta-endorphin: opiate receptor binding activities of six naturally occurring beta-endorphin homologs studied by using tritiated human hormone and naloxone as primary ligands--effects of sodium ion. Proc Natl Acad Sci U S A 1982 Apr;79(7):2191-3.
                doi: 10.1073/pnas.79.7.2191pubmed: 6285371google scholar: lookup
              3. Li CH, Yamashiro D, Nicolas P. Beta-endorphin: replacement of tyrosine in position 27 by tryptophan increases analgesic potency--preparation and properties of the 2-nitrophenylsulfenyl derivative. Proc Natl Acad Sci U S A 1982 Feb;79(4):1042-4.
                doi: 10.1073/pnas.79.4.1042pubmed: 6280164google scholar: lookup