Analysis and Comparison of In Vitro Synthesized Glial Fibrillary Acidic Protein with Rat CNS Intermediate Filament Proteins

Analysis and Comparison of In Vitro Synthesized Glial Fibrillary Acidic Protein with Rat CNS... Abstract: 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Journal of Neurochemistry Wiley

Analysis and Comparison of In Vitro Synthesized Glial Fibrillary Acidic Protein with Rat CNS Intermediate Filament Proteins

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Publisher
Wiley
Copyright
Copyright © 1982 Wiley Subscription Services, Inc., A Wiley Company
ISSN
0022-3042
eISSN
1471-4159
D.O.I.
10.1111/j.1471-4159.1982.tb10863.x
Publisher site
See Article on Publisher Site

Abstract

Abstract: 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.

Journal

Journal of NeurochemistryWiley

Published: Jan 1, 1982

References

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