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Related Experiment Videos

Polymorphism in the coding sequence of the horse transferrin gene

M A Carpenter1, T E Broad

  • 1AgResearch Grasslands Research Centre, Palmerston North New Zealand.

Genome
|February 1, 1994
PubMed
Summary

Horse transferrin exhibits significant genetic variation. Sequencing revealed two distinct groups of transferrin variants, with differences clustered in specific protein regions, aiding in understanding iron transport protein diversity.

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Area of Science:

  • Genetics
  • Biochemistry
  • Molecular Biology

Background:

  • Transferrin is the primary iron transport protein in blood.
  • Transferrin is known for its high degree of polymorphism across various species, including horses.
  • Previous research suggested exons 12 and 15 as potential sites of genetic variation in horse transferrin.

Purpose of the Study:

  • To identify and characterize sequence polymorphisms in horse transferrin variants.
  • To determine the genetic relationships between different horse transferrin alleles.
  • To investigate the structural implications of identified polymorphisms.

Main Methods:

  • DNA sequencing of exons 12 and 15 from different horse transferrin variants (D, R, F1, F2, H2, *, O).
  • Analysis of single-stranded conformation polymorphisms (SSCP) to map allelic differences.

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  • Mapping of polymorphic residues onto the three-dimensional structure of human lactoferrin.

    • Main Results:

    • Ten nucleotide substitutions were identified between D and R variants, resulting in six amino acid replacements.
    • Horse transferrin variants were categorized into two main groups based on sequence analysis.
    • Three nucleotide substitutions, including two amino acid changes, were found between D and F1 alleles.
    • All eight polymorphic residues were located in a concentrated area at one end of the C-lobe of the transferrin structure.

    Conclusions:

    • Horse transferrin variants form two distinct genetic groups.
    • Identified polymorphisms are concentrated in a specific region of the protein structure.
    • These findings contribute to understanding the molecular basis of transferrin diversity and its functional implications in horses.