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Home / Equine Research Bank / Infect Immun / Identification and quantitation of equine serum and secretor...
Infection and immunity1972; 6(4); 610-615; doi: 10.1128/iai.6.4.610-615.1972

Identification and quantitation of equine serum and secretory immunoglobulin A.

Abstract: Immunoglobulin A (IgA) was demonstrated in equine serum and secretions. This immunoglobulin had a molecular weight extending from 150,000 to 700,000 and reacted with specific antihuman alpha-chain antiserum. Antigenic determinants specific for secretory IgA were demonstrated and found to be absent on serum IgA. Antigen binding activity was detected in IgA from tears. Purified IgA was antigenically distinct from equine IgG, IgM, IgG(T), and aggregating immunoglobulin. Quantitative studies demonstrated that IgA was the predominant immunoglobulin in tears and milk but not in colostrum. The electrophoretic mobility, size, presence of secretory component, and reaction with specific antihuman alpha-chain antiserum demonstrates that this immunoglobulin is the equine homologue of human IgA.
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Publication Date: 1972-10-01 PubMed ID: 4117801PubMed Central: PMC422582DOI: 10.1128/iai.6.4.610-615.1972Google Scholar: Lookup
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  • Journal Article

Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

The research article presents findings on the identification and quantification of Immunoglobulin A (IgA) in horse serum and secretions, highlighting its differences from other types of horse immunoglobulins.

Identifying Immunoglobulin A in Equine Serum and Secretions

  • The research focused on the detection of Immunoglobulin A (IgA) in both equine, or horse, serum and secretions. Serum is the clear, pale-yellow liquid that separates from the blood where there are no blood cells or clotting factors. Secretions, on the other hand, include fluids like tears and milk.
  • IgA was identified through its reaction with specific antihuman alpha-chain antiserum, which suggests it shared some similarities with human IgA.
  • The molecular weight of the equine IgA was found to vary between 150,000 to 700,000. Molecular weight is a measure of the size or mass of molecules and can be used to distinguish between different types of immunoglobulins.

Distinguishing Features of Immunoglobulin A

  • The researchers found certain antigenic determinants that were specific to secretory IgA, meaning that these markers were not found on the serum IgA. Antigenic determinants are the parts of the antigen that are recognized and bound by the immune system.
  • Another distinguishing feature of IgA was found in its antigen-binding activity in tears, indicating that this immunoglobulin plays a preferential role in this secretion.
  • The purified IgA was also found to be antigenically distinct from other equine immunoglobulins including IgG, IgM, IgG(T), and the so-called aggregating immunoglobulin.

Quantifying Immunoglobulin A in Equine Secretions

  • The research included quantitative studies that illustrated how IgA was the predominant immunoglobulin in tears and milk, but crucially, not in colostrum. Colostrum is a type of milk produced by mammals that is rich in antibodies and can bolster the immune system of newborns.

Conclusion: Equine Immunoglobulin A as Homologue of Human Immunoglobulin A

  • The combination of the IgA’s electrophoretic mobility (meaning its speed of movement under an electric field), size, inclusion of a secretory component, and its reaction with the specific antihuman alpha-chain antiserum led the researchers to conclude that this IgA is actually the equine homologue, or equivalent, of the human IgA.
  • Such findings can be instrumental in further understanding the immune systems of mammals and exploring potential avenues for immunological inter-species research.

Cite This Article

APA
McGuire TC, Crawford TB. (1972). Identification and quantitation of equine serum and secretory immunoglobulin A. Infect Immun, 6(4), 610-615. https://doi.org/10.1128/iai.6.4.610-615.1972

Publication

Infection and immunity
ISSN: 0019-9567
NlmUniqueID: 0246127
Country: United States
Language: English
Volume: 6
Issue: 4
Pages: 610-615

Researcher Affiliations

McGuire, T C
    Crawford, T B

      MeSH Terms

      • Animals
      • Antibodies, Bacterial
      • Chromatography
      • Colostrum / immunology
      • Epitopes
      • Guinea Pigs
      • Horses / immunology
      • Immunoelectrophoresis
      • Immunoglobulin A / analysis
      • Immunoglobulin A / isolation & purification
      • Immunoglobulin G / analysis
      • Immunoglobulin M / analysis
      • Iodine Isotopes
      • Molecular Weight
      • Rabbits
      • Tears / immunology

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      Citations

      This article has been cited 9 times.
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