In vitro synthesis of two brain-specific proteins (S100 and 14-3-2) by polyribosomes from rat brain
Archives of Biochemistry and Biophysics, ISSN: 0003-9861, Vol: 155, Issue: 1, Page: 58-69
1973
- 44Citations
- 2Captures
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Metrics Details
- Citations44
- Citation Indexes44
- CrossRef44
- 39
- Captures2
- Readers2
Article Description
Free and membrane-bound polyribosomes were prepared from whole brain, cortex, and hindbrain-medullary white matter of young adult rats. In a homologous cell-free system, two brain-specific acidic proteins (S100 and 14-3-2) were identified in the soluble proteins released from the polyribosomes during incubation for 1 hr at 37°C. Both S100 and 14-3-2 proteins were found to be synthesized primarily by free polyribosomes. De novo synthesis of the 14-3-2 protein was achieved in a reconstituted cerebral cell-free system containing polysome-derived DNA-like RNA and 40S+60S subunits. The radioactively labeled S100 and 14-3-2 proteins were identified by immunoprecipitation with specific antisera and sodium dodecyl sulfate polyacrylamide gel electrophoresis. No difference was found in the synthesis of these brain-specific proteins when a hepatic supernatant enzyme fraction was used in the cell-free system containing cerebral polyribosomes. Furthermore, in vitro synthesis of S100 and 14-3-2 proteins did not occur with liver polysomes when a supernatant enzyme fraction from either liver or brain was used.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0003986173800098; http://dx.doi.org/10.1016/s0003-9861(73)80009-8; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0015591990&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/4712448; https://linkinghub.elsevier.com/retrieve/pii/S0003986173800098; http://linkinghub.elsevier.com/retrieve/pii/S0003986173800098; http://api.elsevier.com/content/article/PII:S0003986173800098?httpAccept=text/xml; http://api.elsevier.com/content/article/PII:S0003986173800098?httpAccept=text/plain; http://dx.doi.org/10.1016/s0003-9861%2873%2980009-8; https://dx.doi.org/10.1016/s0003-9861%2873%2980009-8
Elsevier BV
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