title: Stability of tumor necrosis factor-alpha during ion exchange chromatography.
abstract: Denaturation of target protein by various separation and purification steps contributes significant part to the total product loss in bioseparation. The conformational change and accompanying loss of activity of tumor necrosis factor-alpha during ion exchange chromatography was reversible and was decreased by adding polyethylene glycol 200 at 2 to 5% (v/v) to the eluting solution.
authors.affiliation: National Key Laboratory of Biochemical Engineering, Institute of Process Engineering, Chinese Academy of Sciences, P.R. China.
authors.forename: Ming
authors.initials: M
authors.lastname: Li
authors.forename: Yunshan
authors.initials: Y
authors.lastname: Wang
authors.forename: Weijun
authors.initials: W
authors.lastname: Li
authors.forename: Zhiguo
authors.initials: Z
authors.lastname: Su
mesh_terms: D002852:Chromatography, Ion Exchange / Q000379:methods*; D004355:Drug Stability; D011092:Polyethylene Glycols / Q000737:chemistry; D011487:Protein Conformation; D011489:Protein Denaturation; D014409:Tumor Necrosis Factor-alpha / Q000737:chemistry* / Q000302:isolation & purification*
chemical_list: D014409:Tumor Necrosis Factor-alpha; D011092:Polyethylene Glycols