Abstract
Abstract A new procedure is developed for extraction and purification of amyloid proteins from milligram amounts of amyloid-containing tissue. The procedure involves extraction of amyloid proteins with acidic agueous acetonitrile and their purification by size-exclusion high-performance liquid chromatography (HPLC). The molecular weight and type of isolated amyloid proteins were determined by using sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE), followed by immunoblotting technique. The developed procedure is more rapid and requires significantly smaller amount of tissue material (about 10 mg), comparing with the conventional amyloid isolation technique performed by using gram amounts of autopsy specimen. The techniques applied presently may be useful for precise determination of amyloid type in biopsies.
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