Soluble complex formation of bovine immunoglobulin G2 with staphylococcal protein A studied by gel filtration chromatography.
The binding property of bovine IgG2 to staphylococcal Protein A was investigated by the methods of gel filtration chromatography and affinity chromatography. High performance gel filtration chromatography was carried out using TSK gel G3000SW and G2000SW columns, and immobilized Protein A column was used for affinity chromatography. Although bovine IgG2 did not form any precipitin lines with Protein A by double diffusion method on agar gel, IgG2 could bind to immobilized Protein A column. Moreover, by gel filtration chromatography, peaks of the complex between bovine IgG2 and Protein A were observed in addition to the IgG2 monomer peak. Thus, it is concluded that bovine IgG2 interacts with staphylococcal Protein A and forms "soluble complexes". Carbethoxylated IgG2 lost its affinity to Protein A indicating that histidyl residues in IgG2 is essential for the binding to Protein A.
Shimazaki
K
K
Department of Animal Science, Obihiro University of Agriculture, Japan.
D000818:Animals; D002417:Cattle / Q000276:immunology*; D002850:Chromatography, Gel; D003126:Colostrum / Q000276:immunology; D007074:Immunoglobulin G / Q000378:metabolism*; D013205:Staphylococcal Protein A / Q000378:metabolism*
D007074:Immunoglobulin G; D013205:Staphylococcal Protein A