Comparative studies of the high molecular weight amyloid fibril proteins and similar components from normal tissues.
Analysis of purified amyloid fibrils by gel filtration, polyacrylamide gel electrophoresis in SDS and 8 M urea, and immunodiffusion and immunoelectrophoresis showed that, in addition to the specific amyloid proteins AA and AL, the amyloid preparations all contain a high molecular weight complex. The latter protein complex contains fibronectin, a component which reacts with a non-AA specificity of an antiserum to degraded AA amyloid fibrils (termed the 'B' specificity), and a high molecular weight component excluded by a Sepharose 2BCL column. Similar components were found in aqueous extracts of normal tissues prepared by an identical procedure, and these form aggregates of different size in non-dissociating conditions. It is suggested that amyloid fibrils are complexes of a variety of macromolecules in addition to the specific proteins AA and AL.
D000682:Amyloid / Q000276:immunology / Q000302:isolation & purification; D000941:Antigens / Q000032:analysis; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D005779:Immunodiffusion; D007122:Immunoelectrophoresis; D008970:Molecular Weight
D000682:Amyloid; D000941:Antigens