title: Ion exchange chromatography of proteins and clearance of aggregates.
abstract: Clearance of product related aggregates in therapeutic proteins is a major focus of purification process development. A typical purification process will have one or two chromatographic steps that remove these product related aggregates to an acceptable level. Both cation exchange and anion exchange chromatography can provide robust clearance of aggregates. The primary factors that are critical for aggregate clearance are: resin chemistry, binding and elution condition, peak collection and column load factor. This review covers how these factors can be optimized to increase the effectiveness of ion exchange chromatography in removing aggregates.
authors.affiliation: Purification Process Development, Amgen Inc., Seattle, WA 98119-3105, USA. yyigzaw@amgen.com
authors.forename: Y
authors.initials: Y
authors.lastname: Yigzaw
authors.forename: P
authors.initials: P
authors.lastname: Hinckley
authors.forename: A
authors.initials: A
authors.lastname: Hewig
authors.forename: G
authors.initials: G
authors.lastname: Vedantham
mesh_terms: D001702:Biopharmaceutics / Q000379:methods*; D005591:Chemical Fractionation / Q000379:methods; D002852:Chromatography, Ion Exchange / Q000379:methods*; D046912:Multiprotein Complexes / Q000737:chemistry* / Q000302:isolation & purification*; D011506:Proteins / Q000737:chemistry* / Q000302:isolation & purification*; D013678:Technology, Pharmaceutical / Q000379:methods*
chemical_list: D046912:Multiprotein Complexes; D011506:Proteins