Purification and characterization of prokaryotically expressed human interferon-λ2

被引：0
|
作者：
Mingcai Li
Dongyang Huang
机构：
[1] Shantou University Medical College,Allergy and Inflammation Research Institute
[2] Shantou University Medical College,Molecular Biology Center
来源：
Biotechnology Letters | 2007年 / 29卷
关键词：
Antiviral activity; Enterokinase; Interferon-λ2; Ni-NTA affinity chromatography; Recombinant protein;
D O I：
暂无
中图分类号：
学科分类号：
摘要：
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.
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页码：1025 / 1029
页数：4
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