title: Structure and function of immunoglobulin domains. V. Binding, University of immunoglobulin G and fragments to placental membrane preparations.
abstract: Fc receptors have been shown to be present in human placental tissue with properties distinct from those on macrophages and lymphocytes. A single class of receptor was observed with an intrinsic affinity 4X 10(6) M-(1) for human IgG1. The order of affinity for IgG subclasses was IgG1 = IGG1 greater than IgG3 greater than IgG4. IgA and IgM were not bound. Fc from IgG1 bound with the same affinity as the whole molecule and to the same number of receptor sites, 2 X 10 (12)/mg placental protein. IgG1 was no longer boung after mild reduction and alkylation whereas the binding of Fc was unaffected by this treatment. Neithe C3 nor C3, the two domains which comprise the Fc region of IgG1, bound to the placental receptor. This implies that this Fc receptor is unlike those found on most cell surfaces and that plasental binding is an exception to the theory that each domain has evoked to perform independent functions.
mesh_terms: D001665:Binding Sites; D001666:Binding Sites, Antibody; D006801:Humans; D007141:Immunoglobulin Fc Fragments; D007128:Immunoglobulin Fragments; D007074:Immunoglobulin G; D008566:Membranes / Q000378:metabolism; D009194:Myeloma Proteins / Q000378:metabolism; D010920:Placenta / Q000378:metabolism / Q000648:ultrastructure; D013329:Structure-Activity Relationship
chemical_list: D007141:Immunoglobulin Fc Fragments; D007128:Immunoglobulin Fragments; D007074:Immunoglobulin G; D009194:Myeloma Proteins