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. 1983 Jun;52(3):693–701.

Comparative studies of the high molecular weight amyloid fibril proteins and similar components from normal tissues.

D L Scott, G Marhaug, G Husby
PMCID: PMC1536027  PMID: 6409474

Abstract

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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