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

doi:10.1038/nbt1188-1326

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 journal › Article › peer-review

17 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 language	English
Pages (from-to)	1326-1329
Number of pages	4
Journal	Bio/Technology
Volume	6
Issue number	11
DOIs	https://doi.org/10.1038/nbt1188-1326
State	Published - Nov 1988
Externally published	Yes

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title = "Purification and partial characterization of an interleukin 2-pseudomonas exotoxin fusion protein",

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.",

author = "Pascal Ballon and Weber, \{David V.\} and Maurice Gately and Smart, \{John E.\} and Haya Lorberboum-Galski and David Fitzgerald and Ira Pastan",

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AU - Ballon, Pascal

AU - Weber, David V.

AU - Gately, Maurice

AU - Smart, John E.

AU - Lorberboum-Galski, Haya

AU - Fitzgerald, David

AU - Pastan, Ira

PY - 1988/11

Y1 - 1988/11

N2 - 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.

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

Abstract

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