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Biochemical genetics1975; 13(9-10); 643-649; doi: 10.1007/BF00484922

Carbonic anhydrase isozymes in American ponies and riding horses: a new polymorphic high-activity type isozyme.

Abstract: A study of the erythrocyte carbonic anhydrases of 219 American ponies and 76 riding horses has revealed the presence of five variants of the low-activity CA B isozyme and two variants of the high-activity CA C isozyme. The previously undetected variant of CA C was found only in the pony population and had an allele frequency of 8.9%. A family study of animals possessing the CA B variant A2 showed an unexpected high frequency of inheritance.
Publication Date: 1975-10-01 PubMed ID: 812486DOI: 10.1007/BF00484922Google Scholar: Lookup
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  • Journal Article
  • Research Support
  • U.S. Gov't
  • Non-P.H.S.
  • Research Support
  • U.S. Gov't
  • P.H.S.

Summary

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The research investigates different types of carbonic anhydrase, a protein found in red blood cells, in American ponies and riding horses. The researchers found new variants of this protein, one of which was found only in the pony population.

Introduction

  • The study is centered around carbonic anhydrase isozymes, proteins found in the red blood cells (erythrocytes) of animals and humans alike.
  • In horses, particularly ponies and riding horses, these isozymes are involved in important physiological processes such as the transportation of carbon dioxide and the regulation of pH.
  • Understanding the different isozymes, especially new variants, can provide valuable insights into the genetic and physiological diversity of these equine populations.

Methods

  • The scientists studied 219 ponies and 76 riding horses and analyzed their erythrocytes to identify the types of carbonic anhydrase present.
  • The focus was on detecting different ‘variants’ of these isozymes, which essentially refer to different structural, and potentially functional, versions of the protein.

Findings

  • The researchers identified five variants of the low-activity type of carbonic anhydrase, known as CA B, and two variants of the high-activity type, known as CA C.
  • A particularly noteworthy discovery was a completely previously undetected variant of the CA C protein, which was only found in the ponies, not in the riding horses.
  • This new variant showed an allele frequency of 8.9%, suggesting that close to 9% of the ponies carried this protein form in their genetic code.

Implications

  • The discovery of the new high-activity variant in ponies gives a deeper understanding of the genetic diversity in this horse population.
  • By comparing it to the other types of carbonic anhydrase found, researchers might gain insights into the functional implications of these protein variations.
  • The fact that the newly discovered variant was not found in riding horses can also shed light on the distinct genetic heritages of ponies and riding horses.

Cite This Article

APA
Deutsch HF, Bray RP. (1975). Carbonic anhydrase isozymes in American ponies and riding horses: a new polymorphic high-activity type isozyme. Biochem Genet, 13(9-10), 643-649. https://doi.org/10.1007/BF00484922

Publication

ISSN: 0006-2928
NlmUniqueID: 0126611
Country: United States
Language: English
Volume: 13
Issue: 9-10
Pages: 643-649

Researcher Affiliations

Deutsch, H F
    Bray, R P

      MeSH Terms

      • Alleles
      • Animals
      • Carbonic Anhydrases / blood
      • Erythrocytes / enzymology
      • Female
      • Genetic Variation
      • Horses / blood
      • Isoenzymes / blood
      • Male
      • Phenotype

      References

      This article includes 6 references
      1. Deutsch HF, Taniguchi N, Funakoshi S, Hirai H. Distribution of erythrocyte carbonic anhydrase B-type alleles in Japanese farm horses.. Biochem Genet 1972 Jun;6(4):255-62.
        pubmed: 4199802doi: 10.1007/BF00486119google scholar: lookup
      2. Huisman TH, Schroeder WA, Charache S, Bethlenfalvay NC, Bouver N, Shelton JR, Shelton JB, Apell G. Hereditary persistence of fetal hemoglobin. Heterogeneity of fetal hemoglobin in homozygotes and in conjunction with -thalassemia.. N Engl J Med 1971 Sep 23;285(13):711-6.
        pubmed: 5571129doi: 10.1056/NEJM197109232851303google scholar: lookup
      3. Mancini G, Carbonara AO, Heremans JF. Immunochemical quantitation of antigens by single radial immunodiffusion.. Immunochemistry 1965 Sep;2(3):235-54.
        pubmed: 4956917doi: 10.1016/0019-2791(65)90004-2google scholar: lookup
      4. WILBUR KM, ANDERSON NG. Electrometric and colorimetric determination of carbonic anhydrase.. J Biol Chem 1948 Oct;176(1):147-54.
        pubmed: 18886152
      5. Deutsch HF, Funakoshi S, Fujita T, Taniguchi N, Hieai H. Isolation in crystalline form and properties of six horse erythrocyte carbonic anhydrases.. J Biol Chem 1972 Jul 25;247(14):4499-502.
        pubmed: 4625482
      6. Moore MJ, Funakoshi S, Deutsch HF. Human carbonic anhydrases. VII. A new C type isozyme in erythrocytes of American Negroes.. Biochem Genet 1971 Dec;5(6):497-504.
        pubmed: 5000591doi: 10.1007/BF00485667google scholar: lookup

      Citations

      This article has been cited 1 times.
      1. Jabusch JR, Deutsch HF. Sequence of the high-activity equine erythrocyte carbonic anhydrase: N-terminal polymorphism (acetyl-Ser/acetyl-Thr) and homologies to similar mammalian isozymes. Biochem Genet 1984 Apr;22(3-4):357-67.
        doi: 10.1007/BF00484234pubmed: 6428393google scholar: lookup