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Home / Equine Research Bank / J Exp Med / Equine antihapten antibody. The subunits and fragments of an...
The Journal of experimental medicine1967; 125(2); 249-275; doi: 10.1084/jem.125.2.249

Equine antihapten antibody. The subunits and fragments of anti-beta-lactoside antibody.

Abstract: Eight antigenically unique immunoglobulins have been identified in purified equine anti-p-azophenyl-beta-lactoside (Lac) antibody isolated from a single horse. The Fc fragments of the gammaGa-, gammaGb-, gammaGc-, and -gammaA-globulins have been shown to possess unique antigenic determinants. Common gammaG- and gammaA-Fc fragment antigenic determinants, which were absent from the 10Sgamma(1)- and gammaM-globulins, have also been observed. All antibody populations share two antigenically distinct light (B, L) chain variants. The association of anti-Lac antibody with the hapten p-(p-dimethylamino-benzeneazo)-phenyl-beta-lactoside has been measured by equilibrium dialysis and by fluorescence quenching. A variation in the affinity of anti-Lac antibody for hapten has been observed. The affinity of antibody was unaltered by enzymatic removal of the Fc fragments by peptic digestion or dissociation of the two combining sites on the papain 3.5S Fab fragments, indicating that the observed heterogeneity of affinities was not a direct function of the heterogeneity in structure of the Fc fragments. Isolated heavy (A, H) chains of gammaA-anti-Lac antibody have been shown to have retamed affinity for Lac dye by equilibrium dialysis and by analytical ultracentrifugation, employing a combination of schlieren and absorption optics. The heavy (A, H) chains from two physically separable, antigenically distinct antibody populations, isolated from the same animal and having affinity for the same haptenic determinant, have been found to differ in their amino acid composition. Anti-Lac antibody light (B, L) chains have also been shown to be chemically heterogeneous, and contained populations of polypeptide chains possessing, and populations lacking methionine. The relevance of the observed structural heterogeneity of equine anti-Lac antibody to the problem of defining the mechanism of acquisition of immunological specificity is briefly discussed.
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Publication Date: 1967-02-01 PubMed ID: 4959973PubMed Central: PMC2138359DOI: 10.1084/jem.125.2.249Google 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 study explores the structure and function of equine anti-p-azophenyl-beta-lactoside antibody, a kind of antibody found in horses that reacts with a specific component of beta-lactoside. The research shows that the antibody has a complex structure, with different components displaying unique behavior, and that it is capable of binding to its target in different ways, suggesting a level of structural heterogeneity.

Research on Unique Immunoglobulins

  • The study identified eight distinct immunoglobulin types contained within the isolated equine anti-p-azophenyl-beta-lactoside antibody.
  • Interestingly, each of these immunoglobulins displays unique antigenic determinants, meaning each has its own potential for binding with respective target antigens.

Study of Antibody Fragments

  • The Fc fragments – the tail portions of antibody molecules – of these immunoglobulins also present with unique antigenic determinants.
  • It was also found that there are common antigenic determinants present in gammaG- and gammaA-Fc fragments.

Antibody Affinities and Structural Heterogeneity

  • Depending on the associated hapten, the affinity of the antibody for its target changes. This is an important feature as it suggests the level of immune response can vary.
  • The study found that this variation in affinity is not directly related to the structural heterogeneity of the Fc fragments, setting up interesting questions about the origin of this variability.
  • The isolated heavy chains of this antibody have been shown to retain an affinity for Lac dye as demonstrated by equilibrium dialysis and analytical ultracentrifugation – analytical methods for studying molecular interactions.
  • More findings of heterogeneity were found in the amino acid compositions of the heavy chains of the same antibody, further extending the structural diversity of the antibody under study.

    • <!–

  • Basically, the complexity of these antibodies goes beyond simply recognizing and detoxifying foreign substances – they have a degree of structural variability that may influence their activity and affinity for target molecules.

    • –>

Final Observations

  • The light chains of the antibodies were also shown to have chemical heterogeneity, with different populations possessing varying quantities of methionine.
  • All these findings on the structural complexities of the equine anti-Lac antibodies suggest that the mechanism of acquisition of immunological specificity might be more complicated than previously thought.

Cite This Article

APA
Rockey JH. (1967). Equine antihapten antibody. The subunits and fragments of anti-beta-lactoside antibody. J Exp Med, 125(2), 249-275. https://doi.org/10.1084/jem.125.2.249

Publication

The Journal of experimental medicine
ISSN: 0022-1007
NlmUniqueID: 2985109R
Country: United States
Language: English
Volume: 125
Issue: 2
Pages: 249-275

Researcher Affiliations

Rockey, J H

    MeSH Terms

    • Animals
    • Antibodies / analysis
    • Autoanalysis
    • Chromatography, Gel
    • Dialysis
    • Fluorescent Antibody Technique
    • Haptens
    • Horses
    • Immunodiffusion
    • Immunoelectrophoresis
    • Spectrophotometry
    • Ultracentrifugation

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