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Vimentin and 70K Neurofilament Protein Co‐exist in Embryonic Neurones from Spinal Ganglia
Author(s) -
Jacobs Michael,
Choo Qui Lim,
Thomas Clive
Publication year - 1982
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1982.tb05337.x
Subject(s) - neurofilament , vimentin , intermediate filament , isoelectric point , intermediate filament protein , microbiology and biotechnology , biology , cytoskeleton , protein subunit , chemistry , biochemistry , immunohistochemistry , immunology , cell , gene , enzyme
The mesenchymal intermediate filament protein vimentin and the 70K component of neurofilament were detected by two‐dimensional gel electrophoresis in cultures of pure sensory and sympathetic neurones derived from chick embryos. The identities of these neuronal intermediate filament proteins were confirmed by comparison of their molecular weights, isoelectric points, and peptide patterns from limited papain digestions with those of the corresponding proteins from fibroblasts and brain, respectively. A specific antibody to vimentin stained filamenteous structures and colcemid‐induced coils in both neurones and associated satellite cells. In contrast, a specific antibody to the 70K neurofilament protein stained these structures solely in neurones. This neurone‐specific staining, as well as its molecular weight and isoelectric point, distinguishes the 70K neurofilament protein from the 68K neurofilament as sociated protein described by others, which has been claimed to resemble the tubulin assembly protein.