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A method for analysing lymphocyte surface antigens

J Lambris, M Papamichail

    Journal of Immunological Methods
    |January 1, 1980
    PubMed
    Summary
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    This study presents a new method for isolating and characterizing external lymphocyte surface proteins using radioiodination and immunoprecipitation. The technique allows for the analysis of surface antigens and receptor molecules, offering insights into cell surface structures.

    Area of Science:

    • Immunology
    • Biochemistry
    • Cell Biology

    Background:

    • Characterizing lymphocyte surface proteins is crucial for understanding immune cell function.
    • Existing methods for isolating surface proteins can be limited by loss of structural integrity upon solubilization.

    Purpose of the Study:

    • To describe a novel method for isolating and characterizing external lymphocyte surface proteins.
    • To compare the newly developed method with the established galactose oxidase labeling technique.
    • To demonstrate the utility of the method for isolating surface receptor molecules.

    Main Methods:

    • Lymphocytes were labeled with radioactive iodine (125I).
    • Cells were incubated with antilymphocyte serum and solubilized using NP-40.
    • Proteins were precipitated with Staphylococcus aureus and analyzed using SDS-polyacrylamide gel electrophoresis.

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  • Molecular weights were compared to those obtained via galactose oxidase labeling.

    • Main Results:

    • The described method successfully isolated and characterized external lymphocyte surface proteins.
    • The molecular weights of labeled proteins were determined and compared with existing methods.
    • The technique proved effective for isolating surface receptor molecules, even those sensitive to solubilization.

    Conclusions:

    • A robust method for isolating and characterizing lymphocyte surface proteins has been established.
    • This technique offers an alternative for analyzing surface antigens and receptor molecules.
    • The method preserves the integrity of sensitive surface receptor molecules during isolation.