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Affinity chromatography in nonionic detergent solutions.

J B Robinson, J M Strottmann, D G Wick

    Proceedings of the National Academy of Sciences of the United States of America
    |October 1, 1980
    PubMed
    Summary
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    Detergents interfere with anionic dye affinity chromatography by trapping dyes. Adding anionic detergents releases dyes from micelles, enabling effective protein purification, even for particulate enzymes.

    Area of Science:

    • Biochemistry
    • Protein Purification
    • Chromatography

    Background:

    • Anionic dye affinity chromatography is often ineffective with nonionic detergents.
    • Nonionic detergents can interfere with dye-ligand interactions essential for chromatography.

    Purpose of the Study:

    • To investigate the mechanism of interference by nonionic detergents in anionic dye affinity chromatography.
    • To develop a method to overcome this interference for improved protein purification.

    Main Methods:

    • Used lactate dehydrogenase, Cibacron blue F3GA, and Triton X-100 as model systems.
    • Investigated the effect of adding anionic detergents (deoxycholate, sodium dodecyl sulfate) to mixed micelles.

    Main Results:

    Related Experiment Videos

  • Nonionic detergents encapsulate anionic dyes within micelles, preventing enzyme ligation.
  • Anionic detergents displace dyes from micelles, forming mixed micelles and restoring dye activity.
  • This method successfully purified brain particulate cyclic nucleotide phosphodiesterase.

    • Conclusions:

    • Dye encapsulation by nonionic detergents is the primary cause of chromatographic failure.
    • Strategic addition of anionic detergents can resolve this issue without denaturing proteins.
    • This approach enhances the utility of dye affinity chromatography for detergent-extracted proteins.