John R. McDonald, Michael P. Walsh, in Calcium-Binding Proteins in Health and Disease, 1987.

Hydrophobic interaction chromatography (HIC) is a powerful technique used for the purification of proteins in analytical and preparatory applications. Hydrophobic interaction chromatography (HIC) separates biomolecules, under relatively mild conditions, according to differences in their hydrophobicity. The use of aqueous mobile phases in HIC is less likely to disturb protein conformation and results in better activity recovery. Hydrophobic interaction chromatography (HIC) – today a key method in the purification of monoclonal antibodies – involves the separation of protein molecules in their native and biologically active state owing to a differential interaction of these molecules with hydrophobic sites on the surface of a solid support. Hydrophobic interaction chromatography (HIC) is based on non-polar interactions that are induced by high salt mobile phases. Hydrophobic interaction chromatography (HIC) is based on non-polar interactions that are induced by high salt mobile phases. Publisher Summary. Hydrophobic Interaction Chromatography (HIC) is a gentle technique compared to reversed-phase LC for the binding and desorption of hydrophobic proteins. Stationary phases are similar to reversed phase chromatography (RPC) but the density of functional groups is lower. Hydrophobic Interaction Chromatography. This chapter elaborates the Ca 2+ dependent hydrophobic interaction chromatography on phenyl-Sepharose CL-4B that has been used in the identification and isolation of a number of novel, heat-stable and low-molecular weight proteins from bovine brain. HIC is a type of chromatography which exploits the phenomena of the interaction of hydrophobic groups with each other to prevent the interaction with the hydrophilic or polar groups.

Hydrophobic interaction chromatography (HIC) is a versatile method for the purification and separation of biomolecules by using the function of hydrophobicity.

Samples are adsorbed to the resin at relatively high salt concentrations and eluted by applying Author information: (1)Biogen Idec Corporation, Cambridge, Massachusetts, USA. Hydrophilic interaction chromatography is a variation of liquid phase chromatography that overlaps in function with ion chromatography and reversed-phase liquid chromatography. Stationary phases are similar to reversed phase chromatography (RPC) but the density of functional groups is lower. John R. McDonald, Michael P. Walsh, in Calcium-Binding Proteins in Health and Disease, 1987. 2 Corresponding author brendan.oconnor@dcu.ie Abstract Most proteins and large polypeptides have hydrophobic regions at their surface. Publisher Summary. Hydrophobic interaction chromatography (HIC) is a valuable tool used in protein purification applications. These resins are …

Hydrophobic Interaction Chromatography. HIC sorts biomolecules by degree of their surface hydrophobicity. Property Technique Hydrophobicity Hydrophobic interaction chromatography (HIC) Reversed phase chromatography (RPC) Charge Ion exchange chromatography (IEX), chromatofocusing (CF)

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