The Use of Biospecific Elution in Purifying Proteins from Dye-Ligand Adsorbents

  • Robert K. Scopes

Abstract

Elution of protein from dye-ligand adsorbents can be carried out by non-specific means (salt or pH changes), in which case generally poor resolution is achieved. Biospecific elution using natural ligands to the protein can, in the appropriate conditions, achieve a much higher degree of purification. For biospecific (affinity) elution to succeed, the dye must bind at the natural ligand’s site; screening of a range of dyes to find such an interaction may be necessary to achieve optimum results from affinity elution. The use of differential column adsorption with affinity elution can result in a one-step purification of 20 to 100-fold at the first step in many instances.

Keywords

Natural Ligand FEBS Letter Phosphoglycerate Mutase Ionic Strength Range Cibacron Blue F3GA 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Elsevier Science Publishers Ltd 1989

Authors and Affiliations

  • Robert K. Scopes
    • 1
  1. 1.Centre for Protein and Enzyme TechnologyLa Trobe UniversityBundooraAustralia

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