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- Title
Purification and characterization of prokaryotically expressed human interferon-λ2.
- Authors
Mingcai Li; Dongyang Huang
- Abstract
A system for the production of soluble interferon (IFN)-λ2 was developed by fusing the IFN-λ2, NusA protein, polyhistidine and S peptide genes and then expressing the fused product (Nus-His-S-tagged IFN-λ2) in Escherichia coli. The expressed fusion protein was purified by Ni-NTA affinity chromatography. The fusion tag was removed from recombinant IFN-λ2 by cleavage with enterokinase. N-Terminal sequencing confirmed the identity of the purified protein. When compared with commercial IFN-α2b, IFN-λ2 had similar antiviral activity. The production and characterization of biologically active IFN-λ2 will be beneficial for its potential role in clinical applications.
- Subjects
INTERFERONS; ENTEROKINASE; AFFINITY chromatography; ESCHERICHIA coli; RECOMBINANT proteins; ANTIVIRAL agents
- Publication
Biotechnology Letters, 2007, Vol 29, Issue 7, p1025
- ISSN
0141-5492
- Publication type
Article
- DOI
10.1007/s10529-007-9357-y