The expression of antibacterial peptide CM4 in Escherichia coli fused with human soluble B lymphocyte stimulator activing factor

China Biotechnology

2008, Vol. 28

Issue (3): 32-37 DOI:

The expression of antibacterial peptide CM4 in Escherichia coli fused with human soluble B lymphocyte stimulator activing factor

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Abstract

To explore the expression and function of antibacterial peptide CM4, the expression and biological activity of recombinant fusion protein CM4-hsBAFF were studied. The human soluble B lymphocyte stimulator activing factor (hsBAFF) gene was fused to the sequence encoding CM4 to construct an expression vector pET28a (+)/CM4-hsBAFF. The recombinant protein was high expression of soluble recombinant protein in Escherichia coli cells, and existed in the supernatant after sonication. Recombinant fusion protein which was purified through size-exclusion chromatography was identified by SDS-PAGE and Western blot analysis. SDS-PAGE and Western blot indicated that recombinant protein was secreted as a protein of around 22.0 KDa and can be specially recognized anti-hsBAFF antibody. The recombinant protein can be expressed and displays antimicrobial activity.

Key words： antibacterial peptide CM4 hsBAFF expression purification

Received: 14 November 2007 Published: 28 March 2008

ZTFLH:

R392.11

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Cite this article:

. The expression of antibacterial peptide CM4 in Escherichia coli fused with human soluble B lymphocyte stimulator activing factor. China Biotechnology, 2008, 28(3): 32-37.

URL:

https://manu60.magtech.com.cn/biotech/ OR https://manu60.magtech.com.cn/biotech/Y2008/V28/I3/32

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