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 data 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.