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From the Department of Medicine and the Department of Biochemistry, Shinshu University School of Medicine, Matsumoto, Japan.
Amyloid fibril protein was purified from organs of patients with familial amyloid polyneuropathy (Nagano prefecture, Japan). When compared with amyloid fibril protein from primary amyloidosis and secondary amyloidosis, the protein from familial amyloid polyneuropathy was shown to differ in the molecular weight of the subunit. This protein subunit had the same molecular weight as the prealbumin subunit, but had a different amino acid composition: It did not contain tryptophan and cysteine. Amyloid fibril protein from familial amyloid polyneuropathy therefore differed from IgG, AA protein, and prealbumin.
Address correspondence and reprint requests to Dr. Shoji, Department of Medicine, Institute of Adaptation Medicine, Shinshu University School of Medicine, Matsumoto, 390, Japan.
Accepted for publication April 24, 1980.
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