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The hemoglobin polymorphism of the Sardinian wild dwarf horse and the oxygen binding properties of the four different horse hemoglobins.

Abstract: A study was made of the Hb phenotype of the Sardinian dwarfhorse (Equus caballus jara), one of the last surviving wild horse species in Europe. Hb haplotypes and their frequencies were found to be similar to those described in the Arabian horse (BI = 0.551, BII = 0.389, A = 0.036, V = 0.015), which suggests possible introduction onto the island from North Africa. The oxygen binding properties of the whole hemolysates and of the four different horse Hbs, separated by ion-exchange chromatography, were considered with regard to the effect of chloride, 2,3-bisphosphoglycerate and lactate. Results indicate that no differences exist in the four components that characterize horse Hb. The molecular basis of the intrinsically low oxygen affinity and of the weak interaction of horse Hb with 2,3-bisphosphoglycerate is discussed in the light of the primary structure of the molecule.
Publication Date: 1997-03-01 PubMed ID: 9247845
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  • Comparative Study
  • Journal Article
  • Research Support
  • Non-U.S. Gov't

Summary

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The research explores the hemoglobin (Hb) type in the Sardinian dwarf horse, one of the last free-roaming horse species in Europe. The study looks into the likelihood of this breed originating from North Africa due to shared Hb types and frequencies with the Arabian horse. It also investigates the effect of various compounds on the oxygen-binding properties of horse Hb, affirming that the four components representing horse Hb do not differ.

Hemoglobin Phenotype of the Sardinian Dwarf Horse

  • The study started by identifying the hemoglobin or Hb type of the Sardinian dwarf horse (Equus caballus jara). This species is among the last few freely-roaming horse breeds found in Europe.
  • The researchers observed that their Hb haplotypes and frequencies resembled those described in the Arabian horse. This similarity suggests that this species of horse might have originated from North Africa.

Oxygen Binding Properties of Hemoglobin

  • The research further investigated the impact of several compounds on the oxygen-binding properties of horse Hb. These compounds include chloride, 2,3-bisphosphoglycerate and lactate.
  • Results presented no differences in these properties across the four components that characterize horse Hb.

Discussion on the Molecular Basis

  • The investigators gave attention to the discussion of the structural basis for the inherently low oxygen affinity and of the feeble interaction of horse Hb with 2,3-bisphosphoglycerate.
  • The discussion was guided by understanding the primary structure of the molecule, which can offer insights into these phenomena.

Cite This Article

APA
Pellegrini MG, Corda EM, Manca L, Olianas A, Sanna MT, Fais A, Masala B. (1997). The hemoglobin polymorphism of the Sardinian wild dwarf horse and the oxygen binding properties of the four different horse hemoglobins. Ital J Biochem, 46(1), 7-14.

Publication

ISSN: 0021-2938
NlmUniqueID: 0376564
Country: Italy
Language: English
Volume: 46
Issue: 1
Pages: 7-14

Researcher Affiliations

Pellegrini, M G
  • Istituto di Chimica Biologica, Università di Caglian, Italy.
Corda, E M
    Manca, L
      Olianas, A
        Sanna, M T
          Fais, A
            Masala, B

              MeSH Terms

              • Animals
              • Dwarfism / genetics
              • Gene Frequency
              • Haplotypes
              • Hemoglobins / genetics
              • Hemolysis
              • Horses / genetics
              • Humans
              • Italy
              • Linear Models
              • Oxygen / blood
              • Phenotype
              • Polymorphism, Genetic
              • Protein Binding
              • Species Specificity

              Citations

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