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Purification and Partial Characterization of an Interleukin 2-Pseudomonas Exotoxin Fusion Protein

Bio/Technology volume 6, pages 1326–1329 (1988)Cite this article

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.

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Authors and Affiliations

  1. Department of Protein Biochemistry, Roche Research Center, Hoffmann-La Roche Inc., Nutley, NJ, 07110

    Pascal Bailon, David V. Weber & John E. Smart

  2. Department of Immunopharmacology, Roche Research Center, Hoffmann-La Roche Inc., Nutley, NJ, 07110

    Maurice Gately

  3. Laboratory of Molecular Biology, Division of Cancer Biology and Diagnosis, National Cancer Institute, National Institutes of Health, Bethesda, Maryland, 20892

    Haya Lorberboum-Galski, David Fitzgerald & Ira Pastan

Authors
  1. Pascal Bailon
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  2. David V. Weber
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  3. Maurice Gately
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  4. John E. Smart
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  5. Haya Lorberboum-Galski
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  6. David Fitzgerald
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  7. Ira Pastan
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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

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