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Related Experiment Videos

Antibodies reactive with cell surface carbohydrates.

B A Sela, J L Wang, G M Edelman

    Proceedings of the National Academy of Sciences of the United States of America
    |March 1, 1975
    PubMed
    Summary
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    Researchers identified a novel carbohydrate-specific immunoglobulin (CS-Ig) fraction in animal sera. This CS-Ig binds to cell surface carbohydrates, influencing receptor distribution and potentially acting as a mitogen for lymphocytes, offering new research tools.

    Area of Science:

    • Immunology
    • Glycobiology
    • Biochemistry

    Background:

    • Serum contains diverse proteins, including immunoglobulins (Ig) with various binding specificities.
    • Glycoproteins on cell surfaces play critical roles in cellular interactions and signaling.
    • Characterizing novel Ig fractions can reveal new insights into biological recognition mechanisms.

    Purpose of the Study:

    • To isolate and characterize a novel immunoglobulin fraction from animal sera that binds to glycoproteins.
    • To investigate the binding specificity and functional properties of the isolated immunoglobulin fraction.
    • To explore the potential applications of this fraction as a research reagent.

    Main Methods:

    • Fractionation of animal sera using fetuin-coupled Sepharose chromatography.

    Related Experiment Videos

  • Identification of bound proteins using immunoelectrophoresis and zone electrophoresis.
  • Assessment of binding to erythrocytes and mouse tissues.
  • Inhibition assays with various saccharides, glycoproteins, and lipopolysaccharides.
  • Evaluation of effects on splenocyte receptor redistribution and mitogenicity.

    • Main Results:

    • A reproducible low-yield protein fraction, identified as immunoglobulin, was isolated.
    • This immunoglobulin fraction exhibited binding to erythrocytes and various mouse tissues.
    • Binding was inhibited by fetuin, thyroglobulin, a fetuin glycopeptide, and bacterial lipopolysaccharides.
    • Sialic acid, D-galactose, N-acetyl-D-glucosamine, and D-mannose partially inhibited binding to splenocytes.
    • The isolated fraction, termed carbohydrate-specific Ig (CS-Ig), induced receptor redistribution on lymphocytes and showed weak mitogenic activity in chicken and rabbit sera.

    Conclusions:

    • A novel carbohydrate-specific immunoglobulin (CS-Ig) fraction was isolated from animal sera.
    • CS-Ig binds to carbohydrate moieties on cell surfaces and glycoproteins, suggesting a role in carbohydrate recognition.
    • CS-Ig fractions are valuable reagents for studying cell surface carbohydrates, glycoproteins, and their interactions.
    • CS-Ig may have implications in immune responses and cellular signaling pathways involving carbohydrate recognition.