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Analysis and Comparison of In Vitro Synthesized Glial Fibrillary Acidic Protein with Rat CNS Intermediate Filament Proteins
Author(s) -
Bigbee John W.,
Eng Lawrence F.
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.tb10863.x
Subject(s) - glial fibrillary acidic protein , reticulocyte , antiserum , in vitro , microbiology and biotechnology , intermediate filament , polysome , neurofilament , messenger rna , gel electrophoresis , gfap stain , chemistry , protein filament , biochemistry , lysis , protein biosynthesis , translation (biology) , biology , rna , antibody , ribosome , cell , cytoskeleton , gene , immunology , immunohistochemistry
Intermediate filament (IF) proteins from rat spinal cord were analyzed by two‐dimensional gel electrophoresis and compared with the in vitro translation products of a messenger RNA‐dependent reticulocyte lysate system stimulated with 16‐day‐old rat brain polysomes. In two dimensions, the molecular weight 49,000 to 50,000 band of the IF preparation resolved to seven spots, whereas antiserum to glial fibrillary acidic (GFA) protein precipitated only two immediately adjacent radiolabeled in vitro synthesized products, with molecular weights of 49,000 to 50,000. Autoradiographs of two‐dimensional gels of extracted IF proteins incubated with iodinated IgG fraction of GFA protein antiserum showed that all seven spots were recognized by the antiserum. These observations suggest that the primary gene product of GFA protein is modified either by post‐translational processing or experimental artifact.