title: Immunologic and immunohistochemical study of familial amyloid polyneuropathy.
abstract: Amyloid fibril protein was purified from postmortem organs of patients with familial amyloid polyneuropathy. In immunodiffusion tests, the protein reacted with antihuman prealbumin antibody but not with antihuman retinol-binding protein or antihuman immunoglobulin G (IgG). In immunoelectrophoresis, the amyloid fibril protein gave a single line with a slightly faster mobility than prealbumin. Immunohistochemical analysis, using fluorescent and peroxidase-antiperoxidase methods, showed that the amyloid deposits contained antigenic determinants of human retinol-binding protein and IgG but not prealbumin.
mesh_terms: D000682:Amyloid / Q000276:immunology*; D000686:Amyloidosis / Q000235:genetics / Q000276:immunology*; D000939:Epitopes / Q000032:analysis*; D006801:Humans; D007074:Immunoglobulin G / Q000276:immunology; D007158:Immunologic Techniques; D007564:Japan; D009422:Nervous System Diseases / Q000235:genetics / Q000276:immunology*; D011228:Prealbumin / Q000276:immunology; D012177:Retinol-Binding Proteins / Q000276:immunology; D000685:Serum Amyloid A Protein / Q000276:immunology*
chemical_list: D000682:Amyloid; D000939:Epitopes; D007074:Immunoglobulin G; D011228:Prealbumin; D012177:Retinol-Binding Proteins; D000685:Serum Amyloid A Protein