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The Journal of biological chemistry1987; 262(18); 8603-8609;

Structural studies on equine glycoprotein hormones. Amino acid sequence of equine chorionic gonadotropin beta-subunit.

Abstract: The complete amino acid sequence of the beta-subunit of equine chorionic gonadotropin (eCG beta) has been established by both automated Edman and manual 5-dimethylaminonaphthalene-1-sulfonyl-Edman degradations. Specific fragments were produced by cleavage with Staphylococcus aureus V8 protease, trypsin, or dilute HCl. For the sequence analyses of the heavily glycosylated COOH-terminal portion, a chemical deglycosylation procedure with trifluoromethanesulfonic acid was employed. The peptide chain of eCG beta consists of 149 amino acid residues. Five or more oligosaccharide chains are attached to the protein, 1 unit linked by an N-glycosidic bond to asparagine at residue 13 and four or more units linked by O-glycosidic bonds to serine or threonine at residues in the COOH-terminal portion. The carbohydrate-bearing hydroxy amino acids have not yet been rigorously established. As compared to the beta-subunits of the pituitary gonadotropin hormones, lutropin, follitropin, and thyrotropin, eCG beta possesses a glycosylated COOH-terminal extension of about 30 amino acid residues, as does the human chorionic gonadotropin beta-subunit (hCG beta). When the comparison is restricted inside the disulfide bond-containing core (residues 1-110), the beta-subunit of eCG is highly homologous to hCG beta (66%). On the other hand, although the overall structural features closely resemble each other, much less homology exists in the COOH-terminal extensions of eCG beta and hCG beta.
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Publication Date: 1987-06-25 PubMed ID: 3298238
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  • Comparative Study
  • 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 article presents the established complete amino acid sequence of the beta-subunit of equine chorionic gonadotropin, a hormone produced by horses. The study also compares the structure of this hormone to other similar hormones, revealing significant homology but also notable differences.

Amino Acid Sequence of Equine Chorionic Gonadotropin

The fundamental focus of the research paper is the determination of the complete amino acid sequence of the beta-subunit of equine chorionic gonadotropin (eCG beta):

  • Automated Edman and manual 5-dimethylaminonaphthalene-1-sulfonyl-Edman degradations were used to establish the sequence.
  • The eCG beta peptide chain consists of 149 amino acid residues.
  • Researchers used specific proteases, including Staphylococcus aureus V8 and trypsin, to produce the specific fragments necessary for this sequence analysis.

Glycosylation of the Amino Acid Sequence

The paper also delves into details regarding the glycosylation of the sequence:

  • Five or more oligosaccharide chains are attached to the protein.
  • These units are linked by glycosidic bonds to certain residues. One unit is linked by an N-glycosidic bond to the asparagine at residue 13, and four or more units are linked by O-glycosidic bonds to either serine or threonine at residues in the COOH-terminal portion of the sequence.
  • The exact carbohydrate-bearing hydroxy amino acids are yet to be determined.

Comparison with Other Similar Hormone Subunits

The research further compares the beta-subunit of eCG with the beta-subunits of other gonadotropin hormones:

  • eCG beta has a glycosylated COOH-terminal extension of about 30 amino acid residues, similar to the beta-subunit of human chorionic gonadotropin (hCG beta).
  • Within the disulfide bond-containing core (residues 1-110), the eCG beta-subunit has a high homology (66%) with hCG beta, indicating a high degree of similarity between the two.
  • On the other hand, less structural similarity exists within the COOH-terminal extensions of eCG beta and hCG beta, indicating fundamental structural differences between these hormones.

Cite This Article

APA
Sugino H, Bousfield GR, Moore WT, Ward DN. (1987). Structural studies on equine glycoprotein hormones. Amino acid sequence of equine chorionic gonadotropin beta-subunit. J Biol Chem, 262(18), 8603-8609.

Publication

The Journal of biological chemistry
ISSN: 0021-9258
NlmUniqueID: 2985121R
Country: United States
Language: English
Volume: 262
Issue: 18
Pages: 8603-8609

Researcher Affiliations

Sugino, H
    Bousfield, G R
      Moore, W T
        Ward, D N

          MeSH Terms

          • Amino Acid Sequence
          • Animals
          • Chorionic Gonadotropin
          • Gonadotropins, Equine
          • Horses
          • Peptide Fragments / analysis
          • Peptide Hydrolases

          Grant Funding

          • AM-9801 / NIADDK NIH HHS
          • HD-18210 / NICHD NIH HHS

          Citations

          This article has been cited 14 times.
          1. Byambaragchaa M, Park SH, Park MH, Kang MH, Min KS. Enhanced Production and Functional Characterization of Recombinant Equine Chorionic Gonadotropin (rec-eCG) in CHO-DG44 Cells. Biomolecules 2025 Feb 14;15(2).
            doi: 10.3390/biom15020289pubmed: 40001592google scholar: lookup
          2. Byambaragchaa M, Park SH, Kim SG, Shin MG, Kim SK, Hur SP, Park MH, Kang MH, Min KS. Stable Production of a Tethered Recombinant Eel Luteinizing Hormone Analog with High Potency in CHO DG44 Cells. Curr Issues Mol Biol 2024 Jun 15;46(6):6085-6099.
            doi: 10.3390/cimb46060363pubmed: 38921034google scholar: lookup
          3. Byambaragchaa M, Kim SG, Park SH, Shin MG, Kim SK, Kang MH, Min KS. Production of Recombinant Single-Chain Eel Luteinizing Hormone and Follicle-Stimulating Hormone Analogs in Chinese Hamster Ovary Suspension Cell Culture. Curr Issues Mol Biol 2024 Jan 5;46(1):542-556.
            doi: 10.3390/cimb46010035pubmed: 38248337google scholar: lookup
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          7. 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
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