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Genome1994; 37(1); 157-165; doi: 10.1139/g94-020

Polymorphism in the coding sequence of the horse transferrin gene.

Abstract: Transferrin, the iron transport protein of the blood, is highly polymorphic in many species, including the horse. A number of sequence polymorphisms that distinguish several of the variants of horse transferrin are reported here. Previous studies indicated that exons 12 and 15 were likely to be polymorphic. Sequencing regions of exons 12 and 15 from D and R variants revealed 10 nucleotide substitutions that encoded six amino acid replacements. The F1, F2, H2, and * variants were identical to D, and the O variant was almost identical to R, in the regions studied. The data indicated that the horse transferrin variants make up two distinct groups. The positions of differences between the D and F1 alleles were determined by analyzing single-stranded conformation polymorphisms. Sequencing then revealed three nucleotide substitutions, two of which encoded amino acid substitutions. Location of the eight polymorphic residues on the three-dimensional structure of human lactoferrin revealed that all were clustered at one end of the C-lobe.
Publication Date: 1994-02-01 PubMed ID: 8181736DOI: 10.1139/g94-020Google Scholar: Lookup
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  • Journal Article

Summary

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The research presents a study on the variations (polymorphisms) in the sequence of the transferrin gene in horses. It shows that these variations divide horse transferrin into two distinct groups.

Understanding Transferrin Polymorphism

Transferrin is a protein found in blood, tasked with transporting iron around the body. It has been observed to be highly polymorphic (having multiple form variations) in many species, horses included. Its polymorphic nature is highlighted in this research, focusing on several sequence variations that distinguish different variants of horse transferrin.

Variants of Horse Transferrin

  • Prior investigations suggested exons 12 and 15 (segments of the DNA molecule that carry the code for protein formation) to be potential areas of polymorphism.
  • When these sequences from D and R variants of horse transferrin underwent detailed sequencing, the researchers discovered 10 different nucleotide substitutions, resulting in six alterations in the encoded amino acids.
  • Other variants, such as F1, F2, H2, and * variants were found identical to variant D, and the O variant nearly identical to R, in the studied exons.

Classification of Horse Transferrin Variants

  • The gathered data indicated that the variants of horse transferrin fell into two distinct groups, classifying the gene’s polymorphism into two categories.
  • Subtle differences between D and F1 alleles (alternative forms of a gene) were identified by examining single-stranded conformation polymorphisms. This analysis revealed another three nucleotide substitutions, two of which caused changes in the encoded amino acids.

Location of Polymorphic Residues

  • The eight identified polymorphic residues (places where changes occur in the DNA strand) were located on humans’ lactoferrin’s three-dimensional structure. It was noted that all were gathered at one end of the C-lobe, showing a pattern in the placement of these polymorphic areas.

The research navigates through the complex world of gene polymorphism and uncovers important insights about the transferrin gene’s sequence variations, which contribute to the overarching understanding of horse genetics.

Cite This Article

APA
Carpenter MA, Broad TE. (1994). Polymorphism in the coding sequence of the horse transferrin gene. Genome, 37(1), 157-165. https://doi.org/10.1139/g94-020

Publication

ISSN: 0831-2796
NlmUniqueID: 8704544
Country: Canada
Language: English
Volume: 37
Issue: 1
Pages: 157-165

Researcher Affiliations

Carpenter, M A
  • AgResearch Grasslands Research Centre, Palmerston North New Zealand.
Broad, T E

    MeSH Terms

    • Amino Acid Sequence
    • Animals
    • Base Sequence
    • DNA Primers / genetics
    • DNA, Complementary / genetics
    • DNA, Single-Stranded / chemistry
    • DNA, Single-Stranded / genetics
    • Exons
    • Genetic Variation
    • Horses / genetics
    • Molecular Sequence Data
    • Nucleic Acid Conformation
    • Polymorphism, Genetic
    • Protein Conformation
    • Sequence Homology, Amino Acid
    • Transferrin / chemistry
    • Transferrin / genetics

    Citations

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