title: Finnish hereditary amyloidosis. Amino acid sequence homology between the amyloid fibril protein and human plasma gelsoline.
abstract: Amyloid fibrils were isolated from the kidney of a patient with Finnish hereditary amyloidosis. After solubilization of the fibrils in guanidine-HCl, fractionation by gel filtration, and purification by reverse-phase high-performance liquid chromatography, a homogeneous amyloid protein with an apparent Mr of 9000 was obtained. The protein was subjected to enzymatic digestion by trypsin and endoproteinase Lys-C. The amino acid sequences were determined for 6 of the released peptides and they were all found to be identical to the reported, deduced primary structure of human plasma gelsoline in the region of amino acids 235-269. The results show that the amyloid fibril protein in Finnish hereditary amyloidosis represents a new type of amyloid protein that shows amino acid sequence homology with gelsoline, an actin-modulating protein.
authors: Fourth Department of Medicine, University of Helsinki, Finland.
authors: C P
authors: CP
authors: Maury
authors: K
authors: K
authors: Alli
authors: M
authors: M
authors: Baumann
mesh_terms: D000368:Aged; D000595:Amino Acid Sequence; D000686:Amyloidosis / Q000453:epidemiology / Q000235:genetics* / Q000378:metabolism; D002135:Calcium-Binding Proteins / Q000032:analysis* / Q000097:blood; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D005190:Family; D005387:Finland; D018260:Gelsolin; D006801:Humans; D007668:Kidney / Q000032:analysis / Q000378:metabolism*; D008297:Male; D008840:Microfilament Proteins / Q000032:analysis* / Q000097:blood; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000302:isolation & purification; D012689:Sequence Homology, Nucleic Acid; D000685:Serum Amyloid A Protein / Q000302:isolation & purification*
chemical_list: D002135:Calcium-Binding Proteins; D018260:Gelsolin; D008840:Microfilament Proteins; D010446:Peptide Fragments; D000685:Serum Amyloid A Protein