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Plasma membrane isolation on DEAE-Sephadex beads

L J Gotlib, D B Searls

    Biochimica Et Biophysica Acta
    |October 16, 1980
    PubMed
    Summary
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    This study introduces a simplified, rapid, and cost-effective method for purifying plasma membranes from cultured cells using DEAE-Sephadex beads. The new technique offers high recovery of plasma membrane enzymes with minimal contamination, improving cell membrane research.

    Area of Science:

    • Cell Biology
    • Biochemistry
    • Membrane Protein Research

    Background:

    • Isolation of pure plasma membranes is crucial for studying cell surface proteins and functions.
    • Existing methods for plasma membrane purification can be complex, time-consuming, and expensive.
    • Need for a more accessible and efficient purification technique for cultured cell plasma membranes.

    Purpose of the Study:

    • To develop and present a significantly simplified, rapid, and cost-effective method for purifying plasma membranes from cultured cells.
    • To evaluate the efficiency and purity of the plasma membranes isolated using the novel technique.

    Main Methods:

    • Cultured cells are attached to nitrocellulose-treated DEAE-Sephadex beads.
    • Attached cells undergo shearing via hypotonic lysis, vortex agitation, and sonication.

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  • Plasma membranes are then separated from cellular debris and internal membranes.

    • Main Results:

    • The simplified method demonstrates approximately 25% recovery of L-cell plasma membrane marker enzyme activities.
    • Contamination by internal membrane markers is significantly reduced, measuring much less than 1%.
    • The procedure is considerably easier, faster, and less expensive compared to older methods.

    Conclusions:

    • This novel DEAE-Sephadex bead-based method provides an efficient and accessible approach for plasma membrane purification.
    • The technique yields high-purity plasma membranes suitable for various biochemical and cell biology applications.
    • The simplified protocol enhances the feasibility of plasma membrane studies in diverse research settings.