Study on Fused Expression of the IgG-binding Domain of Streptococcal Protein G and Its IgG-binding Activity

China Biotechnology

2009, Vol. 29

Issue (10): 64-68 DOI:

Study on Fused Expression of the IgG-binding Domain of Streptococcal Protein G and Its IgG-binding Activity

HUANG Xue-nian,XU Yang,LI Yan-ping

State Key Laboratory of Food Science and Technology, Sino-Germany Joint Research Institute, Nanchang University, Nanchang 330047, China

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Abstract

The IgG binding domain of Streptococcal Protein G which can selectively immobilizes the Fc regions of immunoglobulin G (IgG) is a kind of good material for oriented immobilization of antibodies in antibody microarrays. Here, genetically engineered three glutathione S-transferase (GST)　fused proteins ,bearing one, two and three B-Domains respectively(GST-GBx). The IgG-bindding ability of GST-GBx was investigated by ELISA. The date revealed that when the B-domain’s quantity of GST-GBx is identical, the GST-GB3 is the most efficient protein among three GST-GBx protein both the capacity and sensibility of binding IgG. The GST-GB2 is the next one and GST-GB1 is the least one. Thus,the GST-GB3 has significantly predominance in comparison to GST-GB2 and GST-GB1.

Key words： Streptococcal Protein G B-domain GST fused proteins IgG-binding ability ELISA

Received: 12 June 2009 Published: 29 October 2009

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HUANG Xue-Nian, HU Yang, LI Yan-Ping. Study on Fused Expression of the IgG-binding Domain of Streptococcal Protein G and Its IgG-binding Activity. China Biotechnology, 2009, 29(10): 64-68.

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https://manu60.magtech.com.cn/biotech/ OR https://manu60.magtech.com.cn/biotech/Y2009/V29/I10/64

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