Encyclopedia of Astrobiology

Living Edition
| Editors: Muriel Gargaud, William M. Irvine, Ricardo Amils, Henderson James Cleaves, Daniele Pinti, José Cernicharo Quintanilla, Michel Viso

Affinity Chromatography

  • Mark Dörr
Living reference work entry
DOI: https://doi.org/10.1007/978-3-642-27833-4_39-2


Affinity chromatography is a (bio-) chemical separation method based on highly specific molecular interactions (affinity) such as between antigens and antibodies, enzymes and substrates, or receptors and ligands. The stationary phase is commonly composed of beads of a gel (e.g., agarose gel) with a covalently bound ligand (e.g., an antibody). Affinity chromatography is currently one of the most powerful separation methods, as it combines the size fractionation capability of gel permeation chromatography with specific, reversible interactions of molecules.


The method was introduced by P. Cuatrecasas, M. Wilchek, and C.B. Anfinsen in 1968 (Cuatrecasas et al. 1968). Pedro Cuatrecasas and Meir Wilchek were jointly rewarded the Wolf Prize in Medicine 1987 for this discovery.

See Also


Stationary Phase Bioorganic Chemistry Size Fractionation Affinity Chromatography Molecular Interaction 
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.

References and Further Reading

  1. Cuatrecasas P, Wilchek M, Anfinsen CB (1968) Selective enzyme purification by affinity chromatography. Proc Natl Acad Sci U S A 61:636–643. doi:10.1073/pnas.61.2.636CrossRefADSGoogle Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 2014

Authors and Affiliations

  1. 1.University of Southern DenmarkOdense MDenmark