Research-Article| Volume 72, ISSUE 3, P702-707, March 1989

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Soluble Complex Formation of Bovine Immunoglobulin G2 with Staphylococcal Protein A Studied by Gel Filtration Chromatography

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      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.


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