Study on Fused Expression of the IgG-binding Domain of Streptococcal Protein G and Its IgG-binding Activity
- VernacularTitle:链球菌G蛋白IgG结合域(GBx)的融合表达及其IgG结合活性的比较分析
- Author:
Xue-Nian HUANG
;
Yang XU
;
Yan-Ping LI
;
- Publication Type:Journal Article
- Keywords:
Streptococcal protein G B-domain GST fused proteins IgG-binding ability ELISA
- From:
China Biotechnology
2006;0(10):-
- CountryChina
- Language:Chinese
-
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.
