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Immunologic and immunohistochemical study of familial amyloid polyneuropathy

Department of Medicine (Drs. Shoji and Tsukada), and Central Laboratories of the University Hospital (Messrs. Kameko and Kato), Shinshu University School of Medicine, Matsumoto, Japan.

Address correspondence and reprint requests to Dr. Shoji, The Department of Medicine, Shinshu University School of Medicine, Matsumoto 390, Japan.

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.

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				J. Ochiai, S. Tobimatsu, T. Kobayashi, T. Kitamoto, T. Kitaguchi, H. Furuya, I. Goto, and Y. Kuroiwa Nonfamilial Prealbumin-Type Amyloid Polyneuropathy Arch Neurol, December 1, 1986; 43(12): 1294 - 1295. [Abstract] [PDF]