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Preparative high-performance liquid affinity chromatography.

D A Small, T Atkinson, C R Lowe

    Journal of Chromatography
    |August 26, 1983
    PubMed
    Summary
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    Researchers developed a new method using Procion Blue MX-R dye for large-scale protein purification. This high-performance liquid affinity chromatography technique efficiently purified lactate dehydrogenase from rabbit muscle extract.

    Area of Science:

    • Biochemistry
    • Chromatography
    • Protein Purification

    Background:

    • Affinity chromatography is crucial for protein purification.
    • Triazine dyes are effective ligands for protein binding.
    • Scaling up analytical chromatography methods to preparative scales can be challenging.

    Purpose of the Study:

    • To develop a preparative-scale purification method for lactate dehydrogenase.
    • To covalently attach Procion Blue MX-R dye to silica for use as an affinity adsorbent.
    • To evaluate the efficiency and yield of the purification process using high-performance liquid affinity chromatography (HPLAC).

    Main Methods:

    • Covalent attachment of Procion Blue MX-R dye to glycol-silylated silica.
    • Adsorbent characterization to determine dye loading (12 μmol dye/g silica).

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  • Large-scale purification of rabbit muscle lactate dehydrogenase using the developed HPLAC system.

    • Main Results:

    • Essentially homogeneous lactate dehydrogenase was obtained.
    • An overall yield of 80% for the purified enzyme was achieved.
    • The method demonstrated high resolution and speed suitable for preparative protein purification.

    Conclusions:

    • Procion Blue MX-R immobilized on silica is an effective adsorbent for large-scale lactate dehydrogenase purification.
    • Triazine dye-HPLAC can be successfully adapted from analytical to preparative protein purification.
    • This approach offers a viable strategy for efficient and scalable purification of proteins.