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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.
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.