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Animal blood groups and biochemical genetics1984; 15(2); 89-101; doi: 10.1111/j.1365-2052.1984.tb01104.x

Heterogeneity of horse transferrin: the role of carbohydrate moiety.

Abstract: Homozygous horse transferrin (Tf O) is highly heterogeneous. In starch gel electrophoresis it gives at least 9 zones. Two main components (2a and 4b) were purified by rivanol and ammonium sulphate precipitation, DEAE-Sephadex chromatography and SP-Sephadex chromatography. Molecular weights of 75 200 and 80 500 for components 2a and 4b, respectively, were determined by sedimentation equilibrium ultracentrifugation. Amino acid compositions of the two components were similar, and there were no differences in the N-terminus (glutamic acid followed by glutamine) and the C-terminus (valine). Differences were found in carbohydrate composition between components 2a and 4b. Component 2a contained 10 moles of sugar components per mole of protein (4 hexoses, 4 hexosamines and 2 sialic acids), while component 4b contained twice the number of both total carbohydrates and individual sugar components. Carbohydrates were identified as mannose and galactose (ratio mannose: galactose approximately equal to 1.5:1), N-acetylglucosamine and N-acetylneuraminic acid. At present it is not clear whether the difference between the two components resides solely in the difference of carbohydrate contents. It is proposed that component 2a has one diantennary glycan, while component 4b has two.
Publication Date: 1984-01-01 PubMed ID: 6497065DOI: 10.1111/j.1365-2052.1984.tb01104.xGoogle Scholar: Lookup
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Summary

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This study focuses on the heterogeneity of horse transferrin, a protein that carries iron in blood plasma. The researchers have identified differences between two main components of this protein, particularly in their carbohydrate composition, but the significance of these discrepancies is not yet clear.

Study Objectives and Process

  • The aim of this research is to explore the heterogeneity of the horse protein called transferrin. More specifically, the study investigates the role of the carbohydrate moiety (a component of the transferrin protein) in this heterogeneity.
  • Through starch gel electrophoresis (a lab technique used to separate proteins), the researchers identified at least nine zones indicating multiple forms of horse transferrin.
  • Out of these, two main components (labelled as 2a and 4b) were isolated for further study using a series of purification stages. These stages involved rivanol and ammonium sulphate precipitation, and two different types of chromatography.

Results and Findings

  • The researchers determined respective molecular weights of 75,200 and 80,500 for components 2a and 4b using a technique called sedimentation equilibrium ultracentrifugation.
  • Upon examining these components, it was found that they had similar amino acid structures, indicating that the fundamental protein structures of 2a and 4b are the same.
  • However, differences were noticed in their carbohydrate contents. Whilst component 2a contained ten molecules of sugar components for every molecule of protein, component 4b had double the number of both total carbohydrates and individual sugar components.
  • The carbohydrates in question were identified as mannose, galactose, N-acetylglucosamine and N-acetylneuraminic acid.
  • Based on the findings, the researchers proposed that component 2a has one diantennary glycan (a specific type of carbohydrate molecule), while component 4b has two diantennary glycans.

Conclusion and Further Study

  • From this research, it is evident that the heterogeneity of horse transferrin lies, at least partially, in the difference in carbohydrate content between the main protein components.
  • However, the exact significance of these differences remains unknown and requires further investigation, as the study points out that it is not clear whether the difference between the two components lies solely in the difference in carbohydrate contents.

Cite This Article

APA
Stratil A, Tomásek V, Bobák P, Glasnák V. (1984). Heterogeneity of horse transferrin: the role of carbohydrate moiety. Anim Blood Groups Biochem Genet, 15(2), 89-101. https://doi.org/10.1111/j.1365-2052.1984.tb01104.x

Publication

ISSN: 0003-3480
NlmUniqueID: 0263344
Country: Netherlands
Language: English
Volume: 15
Issue: 2
Pages: 89-101

Researcher Affiliations

Stratil, A
    Tomásek, V
      Bobák, P
        Glasnák, V

          MeSH Terms

          • Amino Acids / analysis
          • Animals
          • Carbohydrates / analysis
          • Electrophoresis, Starch Gel
          • Homozygote
          • Horses / genetics
          • Molecular Weight
          • Transferrin / genetics
          • Transferrin / isolation & purification

          Citations

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