Prealbumin variants in the amyloid fibrils of Swedish familial amyloidotic polyneuropathy.
Amino-acid sequence analysis of an amyloid fibril protein from a patient with Swedish familial amyloidotic polyneuropathy showed homology with prealbumin but with heterogeneous N-terminal deletions. One-third of the molecules had the same amino acid substitution, methionine for valine in position 30, as in familial amyloidosis of Portuguese, Japanese and Swedish-American type. A protein with the same antigenic properties and size was found in the fibrils of two other patients with Swedish FAP while the amyloid fibrils in two further patients predominantly contained a smaller prealbumin-derived protein. Cyanogen bromide cleavage of this protein revealed no evidence for a methionine residue in position 30.
D000368:Aged; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000682:Amyloid / Q000032:analysis*; D000686:Amyloidosis / Q000235:genetics* / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D006801:Humans; D005779:Immunodiffusion; D008297:Male; D008875:Middle Aged; D009422:Nervous System Diseases / Q000235:genetics* / Q000378:metabolism; D011228:Prealbumin / Q000032:analysis*
D000596:Amino Acids; D000682:Amyloid; D011228:Prealbumin; C041120:amyloid prealbumin