Encyclopedia of Polymeric Nanomaterials

Living Edition
| Editors: Shiro Kobayashi, Klaus Müllen

Affinity Chromatographic Materials

  • Vipul GuptaEmail author
  • Thiprampai Thamamongood
  • Satoshi Sakamoto
  • Hiroshi Handa
  • Yuki Yamaguchi
Living reference work entry
DOI: https://doi.org/10.1007/978-3-642-36199-9_136-1



Affinity signifies the degree to which a molecule associates with another molecule. Affinity chromatography takes advantage of this association to isolate and purify target molecules for the ligand of interest from mixtures. Functional materials used to perform affinity purification of the target molecules are termed as affinity chromatography materials (affinity matrices).

Introduction and Historical Background

Affinity chromatography, one of liquid chromatography techniques, is based on specific and reversible interactions found in biological systems such as antigen–antibody reactions and enzyme–substrate interactions. Affinity chromatography is a practical and useful method capable of selectively isolating and purifying a target molecule from crude mixtures, using a specific binding partner or a ligand [1, 2]. Cell lysates or chemical libraries have been used as crude mixtures containing target molecules for...


Affinity Chromatography Target Molecule Affinity Matrix Schistosoma Japonicum Miniemulsion Polymerization 
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.
This is a preview of subscription content, log in to check access.


  1. 1.
    Urh M, Simpson D, Zhao K (2009) Affinity chromatography: general methods, Chap 26. Methods Enzymol 463:417–438CrossRefGoogle Scholar
  2. 2.
    Schiel JE, Mallik R, Soman S, Joseph KS, Hage DS (2006) Applications of silica supports in affinity chromatography. J Sep Sci 29:719–737CrossRefGoogle Scholar
  3. 3.
    Starkenstein E (1910) Ferment action and the influence upon it of neutral salts. Biochem Z 24:210–218Google Scholar
  4. 4.
    Campbell DH, Luescher E, Lerman LS (1951) Immunologic adsorbents. I. Isolation of antibody by means of a cellulose-protein antigen. Proc Natl Acad Sci 37:575–578. PMCID: PMC1063424wCrossRefGoogle Scholar
  5. 5.
    Lerman LS (1953) A biochemically specific method for enzyme isolation. Proc Natl Acad Sci 39:232–236. PMCID: PMC1063764CrossRefGoogle Scholar
  6. 6.
    Hjerten S (1964) The preparation of agarose spheres for chromatography of molecules and particles. Biochim Biophys Acta 79:393–398CrossRefGoogle Scholar
  7. 7.
    Axén R, Porath J, Ernback S (1967) Chemical coupling of peptides and proteins to polysaccharides by means of cyanogen halides. Nature 214:1302–1304. doi:10.1038/2141302a0CrossRefGoogle Scholar
  8. 8.
    Cuatrecasas P, Wilchek M, Anfinsen CB (1968) Selective enzyme purification by affinity chromatography. Proc Natl Acad Sci 61:636–643. PMCID: PMC225207CrossRefGoogle Scholar
  9. 9.
    Sakamoto S, Hatakeyama M, Ito T, Handa H (2012) Tools and methodologies capable of isolating and identifying a target molecule for a bioactive compound. Bioorg Med Chem 20:1990–2001CrossRefGoogle Scholar
  10. 10.
    Mallik R, Hage DS (2006) Affinity monolith chromatography. J Sep Sci 29:1686–1704CrossRefGoogle Scholar
  11. 11.
    Ayyar BV, Arora S, Murphy C, O’Kennedy R (2012) Affinity chromatography as a tool for antibody purification. Methods 56:116–129CrossRefGoogle Scholar
  12. 12.
    Gustavsson PE, Larsson PO (2006) Support materials for affinity chromatography. In: Hage DS (ed) Handbook of affinity immobilization. CRC press/Taylor and Francis Group, Boca Raton, pp 15–34Google Scholar
  13. 13.
    Zachariou M (ed) (2007) Affinity chromatography, methods and protocols. Humana Press, TotowaGoogle Scholar
  14. 14.
    TOSOH Bioscience. TOYOPEARL instruction manual. Information on methacrylate derivatives “ToyopearlTM” can be obtained from TOSOH CorporationGoogle Scholar
  15. 15.
    Iwaoka E, Mori T, Shimizu T, Hosoya K, Tanaka A (2009) Improvement of monolithic solid material by utilization of spacer for identification of the target using affinity resins. Bioorg Med Chem Lett 19:1469–1472CrossRefGoogle Scholar
  16. 16.
    Sakamoto S, Kabe Y, Hatakeyama M, Yamaguchi Y, Handa H (2009) Development and application of high performance affinity beads: toward chemical biology and drug discovery. Chem Rec 9:66–85CrossRefGoogle Scholar
  17. 17.
    Koneracka M, Kopcansky P, Timbo M, Ramchand CN, Saiyed ZM, Trevan M (2006) Immobilization of enzymes on magnetic particles. In: Guisan JM (ed) Immobilization of enzymes and cells. Humana Press, Totowa, pp 217–228CrossRefGoogle Scholar
  18. 18.
    Genersch E, Eckerskorn C, Lottspeich F, Herzog C, Kühn K, Pöschl E (1995) Purification of the sequence-specific transcription factor CTCBF, involved in the control of human collagen IV genes: subunits with homology to Ku antigen. EMBO J 14:791–800Google Scholar
  19. 19.
    Amersham Biosciences. Affinity chromatography: principles and methods. Edition AC: 18-1022-29Google Scholar
  20. 20.
    Lichty JJ, Malecki JL, Agnew HD, Michelson-Horowitz DJ, Tan S (2005) Comparison of affinity tags for protein purification. Protein Expr Purif 41:98–105CrossRefGoogle Scholar
  21. 21.
    Terpe K (2003) Overview of tag protein fusions: from molecular and biochemical fundamentals to commercial systems. Appl Microbiol Biotechnol 60:523–533CrossRefGoogle Scholar
  22. 22.
    Walls D, Loughran ST (2011) Tagging recombinant proteins to enhance solubility and aid purification. Methods Mol Biol 681:151–175CrossRefGoogle Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 2014

Authors and Affiliations

  • Vipul Gupta
    • 1
    Email author
  • Thiprampai Thamamongood
    • 1
  • Satoshi Sakamoto
    • 1
  • Hiroshi Handa
    • 1
  • Yuki Yamaguchi
    • 1
  1. 1.Department of Biological Information, Graduate School of Bioscience and BiotechnologyTokyo Institute of TechnologyYokohamaJapan