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Human lymphotoxin: purification and some properties.

G A Granger, E C Laserna, W P Kolb

    Proceedings of the National Academy of Sciences of the United States of America
    |January 1, 1973
    PubMed
    Summary
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    Human lymphocytes secrete lymphotoxin, a molecule purified over 4000-fold. This study characterizes lymphotoxin as a large, weakly charged protein with potential heterogeneity, crucial for understanding immune responses.

    Area of Science:

    • Immunology and Molecular Biology
    • Protein Biochemistry

    Background:

    • Lymphotoxin is a key secreted protein produced by human lymphocytes.
    • Understanding its biochemical properties is essential for its role in immune regulation.

    Purpose of the Study:

    • To purify and characterize lymphotoxin from human lymphocytes.
    • To determine the molecular weight, charge, and electrophoretic properties of lymphotoxin.

    Main Methods:

    • Purification using DEAE-cellulose and Sephadex chromatography.
    • Analysis via acrylamide gel electrophoresis and isoelectric focusing.
    • Electrophoretic separation in Pevikon block electrophoresis.

    Main Results:

    • Lymphotoxin was purified 2000- to 4000-fold with 15-25% activity recovery.

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  • Characterized as a weakly charged molecule with a molecular weight of approximately 90,000-100,000.
  • Migrates as a beta- or alpha2 globulin and is separable from other proteins.

    • Conclusions:

    • Lymphotoxin is a distinct macromolecule with specific physicochemical properties.
    • Isoelectric focusing suggests potential limited heterogeneity among lymphotoxin molecules.