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The Journal of membrane biology1982; 64(3); 205-215; doi: 10.1007/BF01870887

Primary structure of horse erythrocyte glycophorin HA. Its amino acid sequence has a unique homology with those of human and porcine erythrocyte glycophorins.

Abstract: The complete amino acid sequence of the major sialoglycoproteins of horse erythrocyte membranes, glycophorin HA, was determined by manual sequencing methods, using tryptic, chymotryptic, and cyanogen bromide fragments. Glycophorin HA is a polypeptide chain of 120 amino acid residues and contains 10 oligosaccharide units attached to the amino-terminal side of the molecule. Its amino terminus is pyroglutamic acid. All of the oligosaccharides are linked O-glycosidically to threonine or serine residues. The amino acid sequence is consistent with the transmembrane orientation of glycophorins. There is no significant homology between the glycosylated domains of horse, human, and porcine glycophorins, but there is a considerable homology between the hydrophobic domains of the three glycophorins, which interact with the lipid bilayer of the erythrocyte membrane.
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Publication Date: 1982-01-01 PubMed ID: 7057453DOI: 10.1007/BF01870887Google Scholar: Lookup
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  • Comparative Study
  • Journal Article

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 involves the analysis of the major sialoglycoproteins of the horse erythrocyte membranes (red blood cells) known as glycophorin HA. The study reveals that the glycophorin HA protein sequence in horses has significant similarities with that in humans and pigs, essentially in their respective hydrophobic regions that interact with the outer membrane of the red blood cells.

Methodology

  • The researchers followed manual sequencing methods to establish the complete amino acid sequence of glycophorin HA.
  • During the analysis, they employed tryptic, chymotryptic, and cyanogen bromide fragments. These are chemical techniques used for breaking down proteins into smaller sequences, which can be individually analyzed.

Key Findings

  • Glycophorin HA was found to be a chain comprised of 120 amino acids. Each of these chains were determined to contain 10 oligosaccharide units.
  • The attachment point of these oligosaccharide units are present on the amino-terminal (the start point) side of the chain.
  • The amino chain starts with a pyroglutamic acid.
  • All of the associated oligosaccharides (a form of complex carbohydrate) are connected through O-glycosidic bonds to either threonine or serine amino acid residues. These are specific types of chemical bonds that occur between a sugar molecule and another molecule (in this case, an amino acid).
  • The overall arrangement and sequence of these amino acids further secures the theory of transmembrane orientation of glycophorins. It substantiates the idea that these proteins extend through the entire thickness of the cell membrane, indicating a significant role in the function of the cell’s surface.

A Comparative Analysis

  • The researchers discovered a high degree of similarity between the hydrophobic (water-repelling) regions of horse, human, and pig glycophorins. These regions interact with the lipid bilayer (fatty layer that forms the cell’s exterior).
  • However, despite this similarity, there was no substantial correlation or homology found between their glycosylated domains. Glycosylation is a modification process that involves adding sugars to proteins – in this case, glycophorins.
  • Thus, the comparative study adds a significant layer to the understanding of the structural and functional aspects of these proteins across different species.

Cite This Article

APA
Murayama JI, Tomita M, Hamada A. (1982). Primary structure of horse erythrocyte glycophorin HA. Its amino acid sequence has a unique homology with those of human and porcine erythrocyte glycophorins. J Membr Biol, 64(3), 205-215. https://doi.org/10.1007/BF01870887

Publication

The Journal of membrane biology
ISSN: 0022-2631
NlmUniqueID: 0211301
Country: United States
Language: English
Volume: 64
Issue: 3
Pages: 205-215

Researcher Affiliations

Murayama, J I
    Tomita, M
      Hamada, A

        MeSH Terms

        • Amino Acid Sequence
        • Animals
        • Carbohydrates / analysis
        • Cyanogen Bromide
        • Glycophorins / isolation & purification
        • Horses
        • Humans
        • Oligosaccharides / analysis
        • Peptide Fragments / analysis
        • Sialoglycoproteins / isolation & purification
        • Species Specificity
        • Swine

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        Citations

        This article has been cited 5 times.
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