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    Home > Biochemistry News > Microbiology News > Purification of Mitochondrial Uracil-DNA Glycosylase Using Ugi-Sepharose Affinity Chromatography

    Purification of Mitochondrial Uracil-DNA Glycosylase Using Ugi-Sepharose Affinity Chromatography

    • Last Update: 2021-02-22
    • Source: Internet
    • Author: User
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    Affinity chromatography is a powerful technique that allows purification of proteins based on biospecific interactions using an affinity absorbent to selectively bind a target protein (
    1
    ,
    2
    ). Separation is achieved through a highly specific, but reversible, interaction with a complementary binding substrate (ligand) that is immobilized on a solid support (matrix). This purification approach has been developed to incorporate protein-protein interactions into the design of the affinity matrix (
    3

    3
    ). Affinity chromatography procedures can achieve purification levels on the order of several thousand-fold in a single separation step. The method presented here utilizes the bacteriophage PBS2 uracil-
    DNA
    glycosylase inhibitor (Ugi) protein as an immobilized ligand on Sepharose 4B beads for purification of mammalian mitochondrial uracil-DNA glycosylase.
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