title: Hydrophobic interaction chromatography to analyze glycoproteins.
abstract: Hydrophobic interaction chromatography (HIC) is one of many separation techniques that can be used to analyze proteins. The separation mechanism is based on the adsorption of the hydrophobic region of the protein to the hydrophobic ligands attached to the column in the presence of high salt. The proteins are then eluted by descending salt concentration. Here we describe the use of this HIC technique to evaluate the hydrophobicity of different monoclonal antibodies (mAbs) and to separate different heterogeneities that occur in mAb.
authors.affiliation: Vaccine Analytical Development, Merck Research Laboratories, West point, PA, USA.
authors.forename: Richard R
authors.initials: RR
authors.lastname: Rustandi
mesh_terms: D000818:Animals; D000911:Antibodies, Monoclonal / Q000737:chemistry / Q000302:isolation & purification*; D016466:CHO Cells; D002853:Chromatography, Liquid / Q000379:methods; D022801:Complementarity Determining Regions / Q000737:chemistry; D006224:Cricetinae; D006023:Glycoproteins / Q000737:chemistry / Q000302:isolation & purification*; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D017434:Protein Structure, Tertiary
chemical_list: D000911:Antibodies, Monoclonal; D022801:Complementarity Determining Regions; D006023:Glycoproteins