Medium-scale ligand-affinity purification of two soluble forms of human interleukin-2 receptor.
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.
Weber
D V
DV
Department of Protein Biochemistry, Roche Research Center, Hoffmann-La Roche Inc., Nutley, NJ 07110.
Keeney
R F
RF
Familletti
P C
PC
Bailon
P
P
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*
D000596:Amino Acids; D008024:Ligands; D015375:Receptors, Interleukin-2; D004247:DNA