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Affinity Precipitation Methods

  • Jane A. Irwin
  • Keith F. Tipton
Part of the Methods in Molecular Biology™ book series (MIMB, volume 59)

Abstract

Affinity chromatography (see  Chapter 16) is a powerful protein purification technique, that exploits the specific interaction between a biological ligand (e.g., a substrate, coenzyme, hormone, antibody, or nucleic acid) or its synthetic analog and its complementary binding site on a protein. One of the variations on this technique (see refs. 1, 2, 3 for reviews) was that of affinity precipitation. As in affinity chromatography, the protein binds to a specific ligand, but the latter is free in solution, rather than bound to an insoluble support. Ligand binding gives rise to the precipitation of the protein from solution, which is then followed by centrifugation. The pellet contains the protein of interest and the ligand, whereas the other components of the mixture remain in the supernatant, allowing easy separation.

Keywords

Potassium Phosphate Buffer Substrate Analog Phenazine Methosulfate HPLC Retention Time Pimelic Acid 
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

© Humana Press Inc. 1996

Authors and Affiliations

  • Jane A. Irwin
    • 1
  • Keith F. Tipton
    • 1
  1. 1.Department of BiochemistryTrinity CollegeDublinIreland

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