In vitro formation of amyloid fibrils from intact beta 2-microglobulin

Biochem Biophys Res Commun. 1985 Sep 30;131(3):1063-8. doi: 10.1016/0006-291x(85)90198-6.

Abstract

Prompted by the identification of hemodialysis-associated amyloid protein as beta 2-microglobulin, we attempted to create in vitro amyloid fibrils from the native protein. Beta 2-microglobulin in PBS was slowly dialyzed free of salt and then concentrated. The residue showed Congophilia with green birefringence by light microscopy and polarization, and non-branching fibrils of indeterminate length, measuring 8 to 10 nm in diameter by electron microscopy, thus meeting the morphologic criteria for amyloid. The present study demonstrates the first successful in vitro creation of amyloid fibrils with intact precursor protein molecules and provides supporting evidence that hemodialysis-associated amyloid is constituted from beta 2-microglobulin.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amyloid / biosynthesis*
  • Chemical Phenomena
  • Chemistry
  • Humans
  • Microscopy, Electron
  • Osmolar Concentration
  • Protein Precursors / metabolism
  • Renal Dialysis
  • Staining and Labeling
  • beta 2-Microglobulin / metabolism*

Substances

  • Amyloid
  • Protein Precursors
  • beta 2-Microglobulin