The effect of aglycosylation on the binding of mouse IgG to staphylococcal protein A

Aglycosylated IgG produced by hybridoma cells cultured in the presence of tunicamycin was compared with normal IgG for its ability to bind to staphylococcal protein A. No differences were found in binding or elution profiles. It is concluded that aglycosylation does not produce major structural alterations at the CH2-CH3 interface of the Fc region of IgG.