ISOLATION AND CHARACTERIZATION OF AMYLOID PROTEINS USING MILLIGRAM AMOUNTS OF AMYLOID-CONTAINING TISSUE

A new procedure is developed for extraction and purification of amyloi d proteins from milligram amounts of amyloid - containing tissue. The procedure involves extraction of amyloid proteins with acidic aqueous acetonitrile and their purification by size-exclusion high-performance liquid chromatography (HPLC). The molecular weight and type of isolat ed amyloid proteins were determined by using sodium dodecyl sulphate p olyacrylamide gel electrophoresis (SDS-PAGE), followed by immunoblotti ng technique. The developed procedure is more rapid and requires signi ficantly smaller amount of tissue material (about 10 mg), comparing wi th the conventional amyloid isolation technique performed by using gra m amounts of autopsy specimen. The techniques applied presently may be useful for precise determination of amyloid type in biopsies.