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Home / Equine Research Bank / J Biol Chem / Demonstration of a COOH-terminal extension on equine lutropi...
The Journal of biological chemistry1985; 260(17); 9531-9533;

Demonstration of a COOH-terminal extension on equine lutropin by means of a common acid-labile bond in equine lutropin and equine chorionic gonadotropin.

Abstract: The beta subunits of equine lutropin and equine chorionic gonadotropin were incubated in 0.013 N HCl for 30 min at 110 degrees C and separated into two fragments by reverse-phase high performance liquid chromatography. The amino acid and carbohydrate compositions of both fragments from each subunit were analyzed. The results demonstrated that equine lutropin-beta has a glycosylated COOH-terminal extension that differs only in carbohydrate composition from the COOH-terminal portion of equine chorionic gonadotropin-beta. This is the first demonstration of a glycosylated COOH-terminal extension in a pituitary glycoprotein hormone.
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Publication Date: 1985-08-15 PubMed ID: 4019483
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  • Journal Article
  • Research Support
  • Non-U.S. Gov't
  • Research Support
  • U.S. Gov't
  • P.H.S.

Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

This research demonstrates the existence of a glycosylated COOH-terminal extension in the hormone equine lutropin, a discovery never made before in a pituitary glycoprotein hormone.

Research Objective and Method

  • The study aimed to identify the structure of equine lutropin and equine chorionic gonadotropin, two vital hormones present in horses. The scientists sought to understand whether equine lutropin has a glycosylated COOH-terminal extension like equine chorionic gonadotropin.
  • The researchers performed this by placing the beta subunits of these hormones in 0.013 N HCl, heating them to 110 degrees Celsius, and then separating into two fragments using reverse-phase high performance liquid chromatography.

Findings

  • After analysis of the amino acid and carbohydrate compositions of both fragments for each subunit, researchers found out that equine lutropin-beta indeed has a glycosylated COOH-terminal extension, similar to the one found in equine chorionic gonadotropin-beta.
  • The only distinction between the COOH-terminal portions of equine lutropin-beta and equine chorionic gonadotropin-beta lies in their carbohydrate composition.

Significance of the Study

  • This research marks the first time a glycosylated COOH-terminal extension has been shown in a pituitary glycoprotein hormone, which broadens the understanding of hormone structure and functionality, particularly in the field of endocrinology and veterinary medicine.
  • The knowledge of differences in carbohydrate composition between equine lutropin-beta and equine chorionic gonadotropin-beta could potentially inform drug development and hormone-based diagnostic tools, and it may help explain any diverse physiological responses triggered by these hormones in horses.

Cite This Article

APA
Bousfield GR, Sugino H, Ward DN. (1985). Demonstration of a COOH-terminal extension on equine lutropin by means of a common acid-labile bond in equine lutropin and equine chorionic gonadotropin. J Biol Chem, 260(17), 9531-9533.

Publication

The Journal of biological chemistry
ISSN: 0021-9258
NlmUniqueID: 2985121R
Country: United States
Language: English
Volume: 260
Issue: 17
Pages: 9531-9533

Researcher Affiliations

Bousfield, G R
    Sugino, H
      Ward, D N

        MeSH Terms

        • Amino Acid Sequence
        • Amino Acids / analysis
        • Animals
        • Chromatography, High Pressure Liquid
        • Gonadotropins, Equine / analysis
        • Horses
        • Luteinizing Hormone / analysis
        • Peptide Fragments / analysis

        Grant Funding

        • AM-09801 / NIADDK NIH HHS
        • HD-18210 / NICHD NIH HHS

        Citations

        This article has been cited 13 times.
        1. Byambaragchaa M, Choi SH, Joo HE, Kim SG, Kim YJ, Park GE, Kang MH, Min KS. Specific Biological Activity of Equine Chorionic Gonadotropin (eCG) Glycosylation Sites in Cells Expressing Equine Luteinizing Hormone/CG (eLH/CG) Receptor.. Dev Reprod 2021 Dec;25(4):199-211.
          doi: 10.12717/DR.2021.25.4.199pubmed: 35141446google scholar: lookup
        2. Antczak DF, Allen WRT. Placentation in Equids.. Adv Anat Embryol Cell Biol 2021;234:91-128.
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        3. Lee SY, Byambaragchaa M, Choi SH, Kang HJ, Kang MH, Min KS. Roles of N-linked and O-linked glycosylation sites in the activity of equine chorionic gonadotropin in cells expressing rat luteinizing hormone/chorionic gonadotropin receptor and follicle-stimulating hormone receptor.. BMC Biotechnol 2021 Sep 5;21(1):52.
          doi: 10.1186/s12896-021-00712-8pubmed: 34482828google scholar: lookup
        4. Byambaragchaa M, Park A, Gil SJ, Lee HW, Ko YJ, Choi SH, Kang MH, Min KS. Luteinizing hormone-like and follicle-stimulating hormone-like activities of equine chorionic gonadotropin β-subunit mutants in cells expressing rat luteinizing hormone/chorionic gonadotropin receptor and rat follicle-stimulating hormone receptor.. Anim Cells Syst (Seoul) 2021;25(3):171-181.
          doi: 10.1080/19768354.2021.1943708pubmed: 34262660google scholar: lookup
        5. Hyun DW, Jeong YS, Lee JY, Sung H, Lee SY, Choi JW, Kim HS, Kim PS, Bae JW. Description of Nocardioides piscis sp. nov., Sphingomonas piscis sp. nov. and Sphingomonas sinipercae sp. nov., isolated from the intestine of fish species Odontobutis interrupta (Korean spotted sleeper) and Siniperca scherzeri (leopard mandarin fish).. J Microbiol 2021 Jun;59(6):552-562.
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        6. Hyun DW, Sung H, Kim PS, Yun JH, Bae JW. Leucobacter coleopterorum sp. nov., Leucobacter insecticola sp. nov., and Leucobacter viscericola sp. nov., isolated from the intestine of the diving beetles, Cybister brevis and Cybister lewisianus, and emended description of the genus Leucobacter.. J Microbiol 2021 Apr;59(4):360-368.
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        8. Oh YJ, Kim JY, Park HK, Jang JY, Lim SK, Kwon MS, Choi HJ. Salicibibacter halophilus sp. nov., a moderately halophilic bacterium isolated from kimchi.. J Microbiol 2019 Nov;57(11):997-1002.
          doi: 10.1007/s12275-019-9421-zpubmed: 31659686google scholar: lookup
        9. Jang JY, Oh YJ, Lim SK, Park HK, Lee C, Kim JY, Lee MA, Choi HJ. Salicibibacter kimchii gen. nov., sp. nov., a moderately halophilic and alkalitolerant bacterium in the family Bacillaceae, isolated from kimchi.. J Microbiol 2018 Dec;56(12):880-885.
          doi: 10.1007/s12275-018-8518-0pubmed: 30361979google scholar: lookup
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          doi: 10.1007/s12275-017-7386-3pubmed: 29214493google scholar: lookup
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          doi: 10.1007/s12275-016-6349-4pubmed: 27572507google scholar: lookup
        12. Hokke CH, Roosenboom MJ, Thomas-Oates JE, Kamerling JP, Vliegenthart JF. Structure determination of the disialylated poly-(N-acetyllactosamine)-containing O-linked carbohydrate chains of equine chorionic gonadotropin.. Glycoconj J 1994 Feb;11(1):35-41.
          doi: 10.1007/BF00732430pubmed: 8193552google scholar: lookup
        13. Stockell Hartree A, Renwick AG. Molecular structures of glycoprotein hormones and functions of their carbohydrate components.. Biochem J 1992 Nov 1;287 ( Pt 3)(Pt 3):665-79.
          doi: 10.1042/bj2870665pubmed: 1445230google scholar: lookup
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