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

1983; Wiley; Volume: 164; Issue: 2 Linguagem: Inglês

10.1016/0014-5793(83)80290-7

1873-3468

Robin J. Leatherbarrow, Raymond A. Dwek,

Protein purification and stability

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 C H 2–C H 3 interface of the Fc region of IgG.