| Literature DB >> 1054847 |
I Gozes, H Schmitt, U Z Littauer.
Abstract
A partially purified fraction of poly(a)-rich brain mRNA coding for tubulin and actin was obtained by stepwise elution from an oligo(deoxythymidylate)-cellulose column and was efficiently translated in a wheat-germ cell-free system. The newly synthesized tubulin and actin migrated along with the authentic proteins on sodium dodecyl sulfate polyacrylamide gels and on sodium dodecyl sulfate-urea polyacrylamide gels, where tubulin alpha- and beta-subunits are separated. The two proteins synthesized in vitro were found to be biologically active; they could be induced to polymerize and were both precipitated by vinblastine. In addition, specific binding of tubulin to an affinity column of colchicine-Sepharose and actin to myosin were demonstrated.Entities:
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Year: 1975 PMID: 1054847 PMCID: PMC432383 DOI: 10.1073/pnas.72.2.701
Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN: 0027-8424 Impact factor: 11.205