PURIFICATION OF GLIAL FILAMENT AND NEUROFILAMENT PROTEINS FROM ACETONE POWDER OF BOVINE SPINAL CORD

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Abstract
Crude neurofilaments, which mainly consist of glial fibrillary acidic protein and neurofilament proteins, were extracted from acetone powder of bovine spinal cord with 0.1 M piperazine-N,N''-bis(2-ethanesulfonic acid) (PIPES) buffer and 1 M acetic acid. Glial fibrillary acidic protein and neurofilament proteins were purified from the crude neurofilaments by ion-exchange chromatography. Sodium dodecylsulfate-polyacrylamide gel electrophoresis, peptide mapping, Western blotting and electron microscopic study showed that these two kinds of intermediate filament proteins retain their native properties. An interesting feature of the reassembled glial filaments was that they often showed helical appearance or double-strand structure.