Cite as: Cold Spring Harb. Protoc.; 2006; doi:10.1101/pdb.prot4201

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Separation of Proteins Using Hydrophobic Interaction Chromatography

Richard J. Simpson and Paul A. O’Farrell

This protocol was adapted from "Hydrophobic Interaction Chromatography," contributed by Richard J. Simpson and Paul A. O’Farrell, Chapter 9, in Purifying Proteins for Proteomics (ed. Simpson). Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, USA, 2004.

The first 15% of the full text of this article appears below.


INTRODUCTION

Hydrophobic interaction chromatography (HIC) is a separation method based on the interactions between proteins and an insoluble, immobilized nonpolar stationary phase. In HIC, the weak hydrophobic interactions between proteins and the nonpolar stationary phase are mediated by high antichaotropic salt concentrations. Protein separations on HIC . . . [Full Text of this Article]


MATERIALS

Reagents

Equipment


METHOD


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