Molecular and General Genetics MGG

, Volume 101, Issue 1, pp 70–81 | Cite as

Ribosomal proteins

III. Preparative separation of Escherichia coli and yeast ribosomal proteins by means of gel filtration
  • Georg Stöffler
  • Victor Rudloff
  • H. G. Wittmann
Article

Summary

Ribosomal proteins of E. coli and yeast were separated by gel filtration on dextran (Sephadex) and polyacrylamide (Bio-Gel) columns. Both gels revealed a valuable separation of the proteins. Finally only Bio-Gel columns were used, since their polyacrylamide matrix is more resistant to the applied organic acids.

The wide distribution of the molecular weights for both the E. coli and yeast ribosomal proteins was confirmed. E. coli ribosomal proteins were separated into three main groups by a single chromatography on Bio-Gel P-10. The same was true for yeast ribosomal proteins. Rechromatography of these protein groups resulted in a further valuable resolution. The fractionated proteins are recovered without any loss and they are very useful for further purification by other procedures, especially on a large scale basis.

Keywords

Molecular Weight Chromatography Purification Filtration Polyacrylamide 

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Copyright information

© Springer-Verlag 1968

Authors and Affiliations

  • Georg Stöffler
    • 1
  • Victor Rudloff
    • 1
  • H. G. Wittmann
    • 1
  1. 1.Max-Planck-Institut für Molekulare GenetikBerlin-DablemGermany

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