Purification of IgG Using Affinity Chromatography on Antigen-Ligand Columns

  • Mark Page
  • Robin Thorpe
Part of the Springer Protocols Handbooks book series (SPH)


Affinity chromatography is a particularly powerful procedure, which can be used to purify IgG, subpopulations of IgG, or the antigen binding fraction of IgG present in serum/ascitic fluid/hybridoma culture supernatant. This technique requires the production of a solid matrix to which a ligand having either affinity for the relevant IgG or vice versa has been bound (1). Examples of ligands useful in this context are:
  1. 1.

    The antigen recognized by the IgG (for isolation of the antigen-specific fraction of the serum/ascitic fluid, and so forth).

  2. 2.

    IgG prepared from an anti-immunoglobulin serum, e.g., rabbit antihuman IgG serum or murine antihuman IgG MAb for the purification of human IgG (see Note 1).

  3. 3.

    IgG-binding proteins derived from bacteria, e.g., protein A (from Staphylococcus aureus Cowan 1 strain) or proteins G or C (from Streptococcus and see Chapter 130).



Sodium Citrate Buffer Fume Hood Guanidine Hydrochloride Trisodium Citrate Cyanogen Bromide 
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  1. 1.
    Hermanson, G. T., Mallia, A. K., and Smith, P. K. (1992) Immobilized Affinity Ligand Techniques. Academic, San Diego, CA.Google Scholar

Copyright information

© Humana Press Inc., Totowa, NJ 1996

Authors and Affiliations

  • Mark Page
    • 1
  • Robin Thorpe
    • 2
  1. 1.MEDEVA, Vaccine Research Unit, Department of BiochemistryImperial College of Science, Technology, and MedicineLondonUK
  2. 2.National Institute for Biological Standards and ControlPotters BarUK

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