Application of receptor-affinity chromatography to bioaffinity purification.
Receptor-affinity chromatography based upon the receptor-ligand interactions has been utilized for the purification of recombinant human interleukin-2 (rIL-2) from microbial and mammalian sources. The receptor-affinity purification process of rIL-2 is used as a model system to demonstrate the utility of this approach for the purification of recombinant proteins. The receptor-affinity purified biomolecule is shown to be biochemically and biologically more homogeneous than the immunoaffinity purified material.
Protein Biochemistry Department, Hoffmann-La Roche Inc., Nutley, NJ 07110.
D V
DV
Weber
P
P
Bailon
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001681:Biological Assay; D002478:Cells, Cultured; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D006863:Hydrogen-Ion Concentration; D007163:Immunosorbent Techniques; D007376:Interleukin-2 / Q000302:isolation & purification*; D008024:Ligands; D051379:Mice; D011955:Receptors, Drug / Q000032:analysis*; D011994:Recombinant Proteins / Q000302:isolation & purification
D000596:Amino Acids; D007376:Interleukin-2; D008024:Ligands; D011955:Receptors, Drug; D011994:Recombinant Proteins