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The Biochemical journal1966; 100(1); 63-68; doi: 10.1042/bj1000063

Comparison of the structure of the immunoglobulins from horse serum.

Abstract: A study of the chemical structure of the horse immunoglobulins IgG and IgA(T) has shown that the amino acid contents of the peptide chains are very similar. These globulins differ most markedly in the products of papain digestion. IgG gives 3.5s products, whereas IgA(T) gives a 5s fraction and smaller components. This difference appears to be associated with the presence of an additional easily reducible disulphide bond in the Fd fragment of the heavy chain. There is two to three times as much carbohydrate in IgA(T) as in IgG. In both, this is in the heavy chain and in IgA(T) more than half is covalently bound to the Fd fragment. The differences in antigenic specificity between horse IgG and IgA(T) appear to be due to structural differences in the Fc fragment.
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Publication Date: 1966-07-01 PubMed ID: 5965260PubMed Central: PMC1265093DOI: 10.1042/bj1000063Google 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.

This research addresses the comparative study of the structure of the immunoglobulins, IgG and IgA(T), present in horse serum. The study involves the inspection of their chemical structures, the dissimilarity of their digestion products and their carbohydrate content.

About Immunoglobulins

  • Immunoglobulins, often known as antibodies, are large Y-shaped proteins. These proteins are involved in immune functioning and are produced by specialized white blood cells called B cells.
  • They identify and bind to specific foreign substances (like bacteria, viruses), tagging them for attack by the immune system.

Chemical Structure of Horse Immunoglobulins

  • The research reveals that the chemical structures of horse immunoglobulins, IgG and IgA(T), are very similar when analyzed for their peptide chains’ amino acid contents.
  • This comparison is significant in understanding the structural similarities and differences in these antibodies, and provides possible insight into their respective functionality.

Digestion Products of Horse Immunoglobulins

  • The products following the digestion of these antibodies with papain, an enzyme known for breaking down proteins, appear to differ significantly.
  • The research shows that digestion of IgG results in 3.5s products, while digestion of IgA(T) yields a larger 5s fraction along with smaller components.
  • This substantial difference is linked to the presence of an easily reducible disulfide bond in the Fd fragment of the heavy chain of IgA(T).

Carbohydrate Presence in Immunoglobulins

  • The study points out that the quantity of carbohydrates in IgA(T) is two to three times more than in IgG.
  • In both immunoglobulins, this carbohydrate component is found in the heavy chain. However, in IgA(T), more than half of it is covalently (chemically) bound to the Fd fragment.

Differences in Antigenic Specificity

  • The key point stressed is the difference in antigenic specificity between horse IgG and IgA(T), which is believed to be attributable to the structural variance in the Fc fragment.
  • This insight could be instrumental in the development of more effective response strategies for infectious diseases in horses, allowing for a better understanding of how these immunoglobulins interact with pathogens.

Cite This Article

APA
Weir RC, Porter RR. (1966). Comparison of the structure of the immunoglobulins from horse serum. Biochem J, 100(1), 63-68. https://doi.org/10.1042/bj1000063

Publication

The Biochemical journal
ISSN: 0264-6021
NlmUniqueID: 2984726R
Country: England
Language: English
Volume: 100
Issue: 1
Pages: 63-68

Researcher Affiliations

Weir, R C
    Porter, R R

      MeSH Terms

      • Amino Acids / analysis
      • Animals
      • Antigens
      • Clostridium
      • Diphtheria Toxin
      • Horses
      • Immune Sera
      • Immunochemistry
      • Immunoelectrophoresis
      • Papain / pharmacology
      • Peptides / analysis
      • Tetanus Toxoid

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      This article includes 18 references
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