Purification and renaturation of recombinant human interleukin-2

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[Purification and renaturation of recombinant human interleukin-2-pseudomonas exotoxin (IL2-PE66(4GLU)) fusion protein].

OBJECTIVE To evaluate the effect of a novel approach for purification and renaturation of recombinant human interleukin-2-pseudomonas exotoxin (IL2-PE66(4Glu)) fusion protein. METHODS A novel purification method established in our laboratory was adopted for the purification of the inclusion body, and after renaturation, recombinant human IL2-PE66(4Glu) fusion protein was purified by DEAE-Seph...

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Optimized conditions for high-level expression and purification of recombinant human interleukin-2 in E. coli.

Interleukin-2 (IL-2), a potent cytokine has been used in anti-cancer therapy for over a decade now. IL-2, originally identified as a growth factor for T lymphocytes is a 15 kDa hydrophobic glycoprotein that induces the activation, clonal proliferation and differentiation of T and B-lymphocytes and enhances the cytotoxicity of monocytes and natural killer (NK) cells. Here, we report a simple met...

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Purification and refolding of Escherichia coli-expressed recombinant human interleukin-2.

The expression of rhIL-2 (recombinant human interleukin-2) in bacteria results in the formation of insoluble inclusion-body aggregates. These aggregates were first solubilized under denaturing conditions (sodium phosphate buffer solution containing 8 M urea and 10 mM 2-mercaptoethanol) and then purified using IMAC (immobilized metal-ion-affinity chromatography). IMAC was used to capture rhIL-2....

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ژورنال

عنوان ژورنال: Biochemical Journal

سال: 1987

ISSN: 0264-6021,1470-8728

DOI: 10.1042/bj2450085