Author: ["Pascal Bailon","David V. Weber","Ronald F. Keeney","Joan E. Fredericks","Cynthia Smith","Philip C. Familletti","John E. Smart"]
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Abstract
We have developed a receptor–affinity method for the rapid and selective purification of recombinant interleukin–2 (rIL–2) based on the specific interactions between a matrix–bound receptor and its soluble protein ligand. Receptor–affinity purified rIL–2 contains only a highly active monomeric form of the lymphokine in contrast to immunoaffinity chromatography where several molecular forms of rIL–2, with varying degrees of biological activity, are recovered.Cite this article
Bailon, P., Weber, D., Keeney, R. et al. Receptor-Affinity Chromatography: A One-Step Purification for Recombinant Interleukin-2. Nat Biotechnol 5, 1195–1198 (1987). https://doi.org/10.1038/nbt1187-1195 