[Bacterial synthesis of the protein G IgG-binding domain of Streptococcus sp. and prospects of its utilization in immunological practice].
The chemical synthesis of a modified gene fragment that codes IgG-binding domain of protein G of Streptococcus sp. (SPG) was done. Two copies of gene fragmentes SPG were cloned into plasmid vector pET-24(a), for expression of recombinant truncated protein G (rSPG) in the culture of Escherichia coli. IgG-binding capacity and specificity for rSPG was confirmed by model assay such interaction in vitro. Basing on the obtained data we affirm that truncated recombinant protein G is able to bind immunoglobulin G in mammalians and can be used for purification of IgG from sera by affinity chromatography or for synthesis of immunoassay conjugates with broad range specificity.
Spyrydonov
V H
VH
Rybal'chenko
D Iu
DIu
Chumak
R M
RM
Martynenko
D L
DL
Mel'nychuk
M D
MD
Mel'nychuk
S D
SD
D001426:Bacterial Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics; D003001:Cloning, Molecular; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000235:genetics; D007124:Immunoenzyme Techniques / Q000379:methods*; D007074:Immunoglobulin G / Q000378:metabolism*; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics; D013291:Streptococcus / Q000235:genetics / Q000378:metabolism*
D001426:Bacterial Proteins; C034284:IgG Fc-binding protein, Streptococcus; D007074:Immunoglobulin G; D011994:Recombinant Proteins