Desorption of immunoglobulins from Protein A-Sepharose CL-4B under mild conditions.
Conditions which permit the dissociation of IgG-staphylococcal protein A interactions without resort to low pH buffers or the use of chaotropic ions are discussed in relation to: (a) the mechanism of the binding reaction; (b) the use of immobilised protein A for purification of cells or removal of immune complexes from serum. Glycyl-tyrosine, glycyl-histidine, glycyl-phenylalanine and tryptophan, representing the class of competing ligand desorbents, and ethylene glycol, an agent which disrupts hydrophobic interactions, were found to be the best desorbents.
D000818:Animals; D000936:Antigen-Antibody Complex; D002846:Chromatography, Affinity / Q000379:methods; D004151:Dipeptides; D006801:Humans; D007074:Immunoglobulin G / Q000302:isolation & purification; D007136:Immunoglobulins / Q000302:isolation & purification*; D007202:Indicators and Reagents; D012685:Sepharose / Q000031:analogs & derivatives; D013205:Staphylococcal Protein A
D000936:Antigen-Antibody Complex; D004151:Dipeptides; D007074:Immunoglobulin G; D007136:Immunoglobulins; D007202:Indicators and Reagents; D013205:Staphylococcal Protein A; C035771:Sepharose CL 4B; D012685:Sepharose