Selective elution of target protein from affinity resins by a simple reductant with a thiol group

Bioorg Med Chem Lett. 2010 Dec 15;20(24):7361-4. doi: 10.1016/j.bmcl.2010.10.053. Epub 2010 Oct 19.


We have made a chance discovery of selective elution of a specific binding protein from affinity resins by mixing them with aqueous solutions of a widely used reductant, 2-mercaptoethanol (2ME), under mild conditions. Our studies suggest this phenomenon would be generic, and could be a powerful method for identification of a specific binding protein. We here exhibit the experimental conditions and successful examples in which target proteins of benzensulfonamide and FK506 were selectively eluted from affinity resins bearing these compounds, while non-specific ones remained.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Carbonic Anhydrase II / chemistry
  • Carbonic Anhydrase II / isolation & purification
  • Chromatography, Affinity
  • Mercaptoethanol / chemistry*
  • Protein Binding
  • Proteins / chemistry
  • Proteins / isolation & purification*
  • Reducing Agents / chemistry*
  • Resins, Synthetic / chemistry*
  • Sulfonamides / chemistry
  • Tacrolimus / chemistry
  • Tacrolimus Binding Protein 1A / chemistry
  • Tacrolimus Binding Protein 1A / isolation & purification


  • Proteins
  • Reducing Agents
  • Resins, Synthetic
  • Sulfonamides
  • Mercaptoethanol
  • Carbonic Anhydrase II
  • Tacrolimus Binding Protein 1A
  • Tacrolimus