Identification of amyloid prealbumin variant in familial amyloidotic polyneuropathy (Japanese type).
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Tawara S, Nakazato M, Kangawa K, Matsuo H, Araki S
Identification of amyloid prealbumin variant in familial amyloidotic polyneuropathy (Japanese type).
Biochem Biophys Res Commun. 1983 Nov 15;116(3):880-8.
- PubMed ID
- 6651852 [ View in PubMed]
- Abstract
Structural studies on an amyloid fibril protein of 14 K daltons (AFj(INO] isolated from a Japanese patient who suffered from familial amyloidotic polyneuropathy were carried out to unambiguously identify its difference from normal human serum prealbumin. Sequence analyses performed by comparing peptide maps prepared from cyanogen bromide fragments and tryptic peptides of purified RCM-amyloid protein with those from RCM-prealbumin indicate that only a valine residue at position 30 in prealbumin is replaced by a methionine residue. Furthermore, it was also proved that AFj(INO) consists of four components; the prealbumin variant and its three related proteins, which are derived by successively accumulated deletion of the N-terminal three amino acid residues (Gly1, Pro2 and Thr3) from the prealbumin variant.