On-column refolding and purification of recombinant human interleukin-1 receptor antagonist (rHuIL-1ra) expressed as inclusion body in Escherichia coli.

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.

journal_name

Biotechnol Lett

journal_title

Biotechnology letters

authors

Tan H,Dan G,Gong H,Cao L

doi

10.1007/s10529-005-8655-5

keywords:

subject

Has Abstract

pub_date

2005-08-01 00:00:00

pages

1177-82

issue

16

eissn

0141-5492

issn

1573-6776

journal_volume

27

pub_type

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