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.
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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
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DOI: https://doi.org/10.1038/nbt1187-1195