Interactions of pig Fab mu and Fab alpha fragments with protein A from Staphylococcus aureus.
Forty % of serum IgM and 47% of dimeric colostral IgA were bound to protein A-Sepharose. Fab mu and Fab alpha fragments showed a reactivity similar to that of the whole immunoglobulins. Complete elutions of IgM and IgA from the protein A-Sepharose were obtained in lower cocentrations of MgCl2 than the complete elution of IgG. However, IgM and IgA were completely eluted at higher concentrations of MgCl2 in the presence of IgG than in its absence.
D000818:Animals; D002846:Chromatography, Affinity; D007070:Immunoglobulin A / Q000378:metabolism*; D007140:Immunoglobulin Fab Fragments; D007075:Immunoglobulin M / Q000378:metabolism*; D007137:Immunoglobulin alpha-Chains; D007148:Immunoglobulin mu-Chains; D008274:Magnesium / Q000494:pharmacology; D013205:Staphylococcal Protein A / Q000378:metabolism*; D013552:Swine
D007070:Immunoglobulin A; D007140:Immunoglobulin Fab Fragments; D007075:Immunoglobulin M; D007137:Immunoglobulin alpha-Chains; D007148:Immunoglobulin mu-Chains; D013205:Staphylococcal Protein A; D008274:Magnesium