title: Medium-scale ligand-affinity purification of two soluble forms of human interleukin-2 receptor.
abstract: Recombinant technology has facilitated the production of two soluble forms of human interleukin-2 receptor (IL-2R) in Chinese hamster ovary cells. We have developed a ligand-affinity method for the medium-scale purification of these two IL-2Rs, based on the biochemical interactions between the matrix-bound ligand (interleukin-2) and its soluble receptor. The affinity-purified IL-2R is further purified by anion-exchange chromatography followed by gel filtration. This method has provided enough highly pure IL-2R for structure and function studies and for use in practical applications such as high-flux drug screening assays and the receptor-affinity purification of human recombinant interleukin-2.
authors.affiliation: Department of Protein Biochemistry, Roche Research Center, Hoffmann-La Roche Inc., Nutley, NJ 07110.
authors.forename: D V
authors.initials: DV
authors.lastname: Weber
authors.forename: R F
authors.initials: RF
authors.lastname: Keeney
authors.forename: P C
authors.initials: PC
authors.lastname: Familletti
authors.forename: P
authors.initials: P
authors.lastname: Bailon
mesh_terms: D000596:Amino Acids / Q000032:analysis; D002846:Chromatography, Affinity; D004247:DNA / Q000032:analysis; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D008024:Ligands; D008970:Molecular Weight; D015375:Receptors, Interleukin-2 / Q000302:isolation & purification*
chemical_list: D000596:Amino Acids; D008024:Ligands; D015375:Receptors, Interleukin-2; D004247:DNA