AMYLOID FIBRIL PROTEIN IN TYPE-I FAMILIAL AMYLOIDOTIC POLYNEUROPATHY IN JAPANESE

  • 1 January 1981
    • journal article
    • research article
    • Vol. 98  (6) , 811-822
Abstract
Amyloid fibrils were isolated from the kidneys of 2 Japanese patients with type I FAP [familial amyloidotic polyneuropathy] and fractionated on Sephadex G-100 gel column. The elution pattern showed 3 peaks. MW of the 3rd peak protein was about 14,000, which was absent in the chromatogram obtained from the tissue of a nonamyloidotic patient. Antisera raised against whole denatured amyloid fibril components reacted with this protein, giving rise to a precipitin arc on immunoelectrophoretic analysis in the area almost corresponding to prealbumin [PreA] but slightly cathodal to it. The amino acid composition of this protein was different from those of AA protein [amyloid protein of unknown origin], AL protein [amyloid protein from L chain] or normal human PreA subunit. The major subunit GAM III [denatured amyloid protein with guanidine HCl] of amyloid fibril protein (AFj) appears immunologically related to PreA.