Purification and characterization of eukaryotic polypeptide chain initiation factor 4F from Drosophila melanogaster embryos.

@article{Zapata1994PurificationAC,
  title={Purification and characterization of eukaryotic polypeptide chain initiation factor 4F from Drosophila melanogaster embryos.},
  author={Juan Zapata and Miguel {\'A}ngel Mart{\'i}nez and Jos{\'e} Manuel Sierra},
  journal={The Journal of biological chemistry},
  year={1994},
  volume={269 27},
  pages={18047-52}
}
The eukaryotic polypeptide chain initiation factor 4F (eIF-4F), purified by m7GTP-Sepharose chromatography from whole extracts of Drosophila melanogaster embryos, consists of two subunits, the previously identified eIF-4E (35 kDa) (Maroto, F. G., and Sierra, J. M. (1989) Mol. Cell. Biol. 9, 2181-2190) and another of 200 kDa. Both subunits cosedimented through a sucrose density gradient containing 0.5 M KCl. In contrast to rabbit reticulocyte eIF-4F, we did not find any RNA-dependent ATPase… CONTINUE READING
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