Introduction

For purification of proteins and macromolecules

Hydrophobic Interaction Chromatography (HIC) is a method which separates proteins on the basis of their differential interactions with a mildly hydrophobic surface. HIC media are porous chromatography particles, manufactured from crosslinked cellulose to which either a butyl, phenyl or octyl functionality has been covalently bonded via a short spacer. Factors which affect hydrophobic interactions include: salt concentrations, temperature, pH, surfactant and organic solvents. Usually the higher the ionic strength (salt concentration) the stronger the hydrophobic bond. Consequently the interaction is enhanced by conditions inverse to that of ion exchange chromatography. HIC is, therefore, an effective complementary tool for separating and purifying substances which are difficult or cannot be separated by ion exchange.

Features •

 Spherical particles exhibiting high mechanical strength • Butyl and Phenyl functionality • Pre-swollen • Virtually no shrinkage or swelling • Stable in organic solvents and surfactants • Stable coupling chemistry • Resistant to 0.2 M NaOH • Autoclavable (121 °C, 20 min)

Benefits •

High flow rates allowing rapid chromatography and direct scale-up • Enables optimum selectivity to be obtained • Easy packing • Easy large scale operation. No shrinkage at high salt concentrations • Enables range of solvent systems to be utilized • Resistant to cleaning and elution conditions • Sterilizable • Regulatory support