Author(s): Firer MA
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Abstract Many elution buffers are in use for the retrieval of proteins from affinity columns. While the aim of these buffers is to dissociate the various chemical bonds that make up protein-protein interactions and return the target protein to the mobile phase in active form, there is considerable difference of opinion as to which buffer is more suitable for particular applications. This review examines the chemical effect of various elution buffers on protein-protein interactions in the context of affinity chromatography and examines strategies that may be used for selection of an appropriate buffer.
This article was published in J Biochem Biophys Methods
and referenced in Pharmaceutica Analytica Acta