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Home / Equine Research Bank / Glycoconj J / Structure determination of the disialylated poly-(N-acetylla...
Glycoconjugate journal1994; 11(1); 35-41; doi: 10.1007/BF00732430

Structure determination of the disialylated poly-(N-acetyllactosamine)-containing O-linked carbohydrate chains of equine chorionic gonadotropin.

Abstract: The disialylated poly-(N-acetyllactosamine)-containing O-linked oligosaccharide alditols, released by alkaline borohydride treatment of the enzymically N-deglycosylated beta-subunit of equine chorionic gonadotropin, were purified by fast protein liquid chromatography (FPLC) on Mono Q and analysed by fast ion bombardment mass spectrometry (FAB-MS) and 1H-NMR spectroscopy. The identified oligosaccharide alditols have the following structure: [Formula: see text]
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Publication Date: 1994-02-01 PubMed ID: 8193552DOI: 10.1007/BF00732430Google Scholar: Lookup
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  • Journal Article
  • Research Support
  • Non-U.S. Gov't

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.

The research study is about the analysis and determination of the structure of a specific carbohydrate chain found in equine chorionic gonadotropin, a hormone produced by pregnant mares.

Study Background

  • The research focuses on a detailed analysis of a complex carbohydrate, called a poly-(N-acetyllactosamine)-containing O-linked carbohydrate chain, that is found in equine chorionic gonadotropin.
  • Equine chorionic gonadotropin is a hormone produced by pregnant mares and has potential applications in equine reproduction.
  • The specific carbohydrate chain being examined is called a disialylated poly-(N-acetyllactosamine)-containing O-linked carbohydrate chain, which contributes to the overall functionality and properties of the hormone.

Methods and Procedures

  • The researchers isolated the desired carbohydrate chains from the hormone by using an alkaline borohydride treatment on the deglycosylated beta-subunit of equine chorionic gonadotropin.
  • These isolated chains were then purified using a method called fast protein liquid chromatography (FPLC), which allows the separation and purification of these complex molecules.
  • The purified molecules were then analysed using fast ion bombardment mass spectrometry (FAB-MS) and proton nuclear magnetic resonance spectroscopy (1H-NMR). These techniques help identify and characterise the structure of complex molecules, like carbohydrate chains.

Findings and Conclusions

  • Through the rigorous procedures of purification and analysis, they were able to determine the structure of the oligosaccharide alditols, a type of carbohydrate molecule.
  • The research team successfully identified and determined the structure of the disialylated poly-(N-acetyllactosamine)-containing O-linked oligosaccharide alditols of equine chorionic gonadotropin.
  • The detailed analysis and description of this carbohydrate chain’s structure may contribute to a deeper understanding of the hormone’s functionality, particularly in equine reproduction.

Cite This Article

APA
Hokke CH, Roosenboom MJ, Thomas-Oates JE, Kamerling JP, Vliegenthart JF. (1994). Structure determination of the disialylated poly-(N-acetyllactosamine)-containing O-linked carbohydrate chains of equine chorionic gonadotropin. Glycoconj J, 11(1), 35-41. https://doi.org/10.1007/BF00732430

Publication

Glycoconjugate journal
ISSN: 0282-0080
NlmUniqueID: 8603310
Country: United States
Language: English
Volume: 11
Issue: 1
Pages: 35-41

Researcher Affiliations

Hokke, C H
  • Bijvoet Center, Department of Bio-Organic Chemistry, Utrecht, The Netherlands.
Roosenboom, M J
    Thomas-Oates, J E
      Kamerling, J P
        Vliegenthart, J F

          MeSH Terms

          • Amino Sugars / chemistry
          • Animals
          • Carbohydrate Sequence
          • Chorionic Gonadotropin / chemistry
          • Galactitol / analogs & derivatives
          • Glycoproteins / chemistry
          • Horses
          • Molecular Sequence Data
          • Oligosaccharides / chemistry
          • Sequence Analysis
          • Sialic Acids / chemistry
          • Spectrometry, Mass, Fast Atom Bombardment

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          This article includes 11 references
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          Citations

          This article has been cited 5 times.
          1. Rodríguez MC, Mussio PE, Villarraza J, Tardivo MB, Antuña S, Fontana D, Ceaglio N, Prieto C. Physicochemical Characterization of a Recombinant eCG and Comparative Studies with PMSG Commercial Preparations.. Protein J 2023 Feb;42(1):24-36.
            doi: 10.1007/s10930-023-10092-xpubmed: 36652139google scholar: lookup
          2. 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
          3. Jaiman A, Thattai M. Golgi compartments enable controlled biomolecular assembly using promiscuous enzymes.. Elife 2020 Jun 29;9.
            doi: 10.7554/eLife.49573pubmed: 32597757google scholar: lookup
          4. Bhardwaj A, Nayan V, Sharma P, Kumar S, Pal Y, Singh J. Molecular characterization, modeling, in silico analysis of equine pituitary gonadotropin alpha subunit and docking interaction studies with ganirelix.. In Silico Pharmacol 2016 Dec;5(1):5.
            doi: 10.1007/s40203-017-0025-1pubmed: 28721542google scholar: lookup
          5. Vliegenthart JF. The complexity of glycoprotein-derived glycans.. Proc Jpn Acad Ser B Phys Biol Sci 2017;93(2):64-86.
            doi: 10.2183/pjab.93.005pubmed: 28190870google scholar: lookup
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