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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.
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Received: 12 June 2009
Published: 29 October 2009
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