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The effect of aglycosylation on the binding of mouse IgG to staphylococcal protein A
Author(s) -
Leatherbarrow Robin J.,
Dwek Raymond A.
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)80290-7
Subject(s) - chemistry , protein a , tunicamycin , immunoglobulin g , antibody , staphylococcus aureus , microbiology and biotechnology , biochemistry , biology , immunology , bacteria , genetics , unfolded protein response , endoplasmic reticulum
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.