- On-column refolding and purification of recombinant human interleukin-1 receptor antagonist (rHuIL-1ra) expressed as inclusion body in Escherichia coli.
On-column refolding and purification of recombinant human interleukin-1 receptor antagonist (rHuIL-1ra) expressed as inclusion body in Escherichia coli.
Biotechnology letters (2005-09-15)
Haidong Tan, Guoping Dan, Huiying Gong, Lijun Cao
PMID16158260
ABSTRACT
Recombinant human interleukin-1 receptor antagonist (rHuIL-1ra) was produced in E. coli as an inclusion body. rHuIL-1ra was purified to Over 98% purity by anion exchange chromatography after on-column refolding. The optimized processes produced more than 2 g pure refolded rHuIL-1ra per 1 l culture, corresponding to a 44% recovery, without an intermediate dialysis step. Refolded rHuIL-1ra had full biological activity with the MTT assay. An intramolecular disulfide linkage in the oxidized recombinant protein was suggested by data from HPLC and non-reducing SDS-PAGE.
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