Purification and partial characterization of an interleukin 2-pseudomonas exotoxin fusion protein

Pascal Ballon*, David V. Weber, Maurice Gately, John E. Smart, Haya Lorberboum-Galski, David Fitzgerald, Ira Pastan

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

16 Scopus citations

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.

Original languageAmerican English
Pages (from-to)1326-1329
Number of pages4
JournalBio/Technology
Volume6
Issue number11
DOIs
StatePublished - Nov 1988
Externally publishedYes

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