Author: ["Pascal Bailon","David V. Weber","Maurice Gately","John E. Smart","Haya Lorberboum-Galski","David Fitzgerald","Ira Pastan"]
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Abstract
The interleukin-2-Pseudomonas exotoxin (IL2-PE40) is a 54.4 kDa chimeric protein in which the cell recognition domain of Pseudomonas exotoxin is replaced by interleukin-2. It is a potential cytotoxic agent for cells bearing interleukin-2 receptors. We report here the purification of recombinant IL2-PE40 from E. coli extracts by the use of receptor-affinity chromatography. The purified material is homogeneous by various criteria, and the IL2-PE40 preparation contains no detecti-ble level of endotoxin. It should thus be suitable for preclinical and clinical testing.Cite this article
Bailon, P., Weber, D., Gately, M. et al. Purification and Partial Characterization of an Interleukin 2-Pseudomonas Exotoxin Fusion Protein. Nat Biotechnol 6, 1326–1329 (1988). https://doi.org/10.1038/nbt1188-1326 