Isolation of immunoglobulin G by affinity chromatography using an IgG Fc receptor protein from Streptococcus dysgalactiae coupled to a solid phase.
A culture of Streptococcus dysgalactiae (C 26) was shown to bind only to 125I-IgG, whereas another S. dysgalactiae culture (C 12) bound both 125I-IgG and 125I-albumin. The IgG-binding proteins could be readily solubilized by lysozyme treatment of the bacteria and isolated by affinity chromatography on IgG Sepharose. The purified IgG-binding protein from S. dysgalactiae C 26, which lacked simultaneous albumin binding activity, precipitated with IgG preparations from man, cow, horse, pig and mouse but not with chicken IgG. This IgG-binding protein was coupled to CNBr-activated Sepharose and subsequently used for the purification of IgG from both bovine and human serum. SDS-PAGE and immunoelectrophoretic studies confirmed the purity of the eluted proteins.
Lämmler
C
C
Institut für Baketeriologie und Immunologie, Justus-Liebig-Universität, Giessen, F.R.G.
Sting
R
R
D000818:Animals; D001426:Bacterial Proteins / Q000302:isolation & purification* / Q000378:metabolism; D001665:Binding Sites; D015153:Blotting, Western; D002352:Carrier Proteins / Q000378:metabolism; D002846:Chromatography, Affinity; D006801:Humans; D005779:Immunodiffusion; D007122:Immunoelectrophoresis; D007074:Immunoglobulin G / Q000302:isolation & purification* / Q000378:metabolism; D013291:Streptococcus / Q000378:metabolism*
D001426:Bacterial Proteins; D002352:Carrier Proteins; C034284:IgG Fc-binding protein, Streptococcus; D007074:Immunoglobulin G