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An improved purification method for cytoplasmic dynein.

M M Pratt, S Hisanaga, D A Begg

    Journal of Cellular Biochemistry
    |January 1, 1984
    PubMed
    Summary
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    A new, faster method purifies cytoplasmic dynein from sea urchin eggs. This improved protocol uses different chromatography techniques, making dynein purification more efficient for further research.

    Area of Science:

    • Cell Biology
    • Molecular Motors
    • Protein Purification

    Background:

    • Cytoplasmic dynein is a crucial motor protein involved in intracellular transport.
    • Previous purification methods were time-consuming and less efficient.
    • Sea urchin eggs are a valuable source for studying dynein.

    Purpose of the Study:

    • To develop an improved and more efficient method for purifying cytoplasmic dynein.
    • To characterize the enzymatic and structural properties of the purified cytoplasmic dynein.
    • To enable dynein research in systems with limited starting material.

    Main Methods:

    • Substitution of DEAE-cellulose for hydroxylapatite chromatography.
    • Elimination of sucrose density gradient centrifugation.

    Related Experiment Videos

  • Use of phosphocellulose chromatography for purification.

    • Main Results:

    • The new protocol significantly reduces purification time (to 2 days) and increases efficiency.
    • Purified cytoplasmic dynein shares enzymatic properties with axonemal dynein.
    • The purified dynein consists of two high molecular weight polypeptides and three lower molecular weight bands.

    Conclusions:

    • This rapid and efficient purification method facilitates cytoplasmic dynein research.
    • The method is adaptable for limited starting materials like tissue culture cells and nerve axoplasm.
    • Further investigation into cytoplasmic dynein functions is now more accessible.