title: The IgG binding function of the normal red cell plasma membrane: identification of integral polypeptides that bind IgG.
abstract: Non-immune IgG binds to red cell integral membrane proteins obtained by mild alkaline extraction of ghosts. Detergent gel chromatography and electrophoretic analyses of IgG-membrane protein complexes obtained by nonionic detergent solubilization and affinity binding to protein A indicate that three polypeptides participate in the binding of IgG. These have apparent molecular weights of 90 000, 44 000 and 22 000 and are present in a 1:3:0.9 stoichiometry. Evidence obtained indicates that the major sialoglycoproteins are not involved in this type of binding.
mesh_terms: D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D004910:Erythrocyte Membrane / Q000378:metabolism*; D004912:Erythrocytes / Q000378:metabolism*; D006801:Humans; D007074:Immunoglobulin G / Q000378:metabolism*; D008565:Membrane Proteins / Q000378:metabolism*; D008970:Molecular Weight; D010455:Peptides / Q000097:blood; D011485:Protein Binding
chemical_list: D007074:Immunoglobulin G; D008565:Membrane Proteins; D010455:Peptides