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Ribosomal proteins

I. Isolation, amino acid composition, molecular weights and peptide mapping of proteins from E. coli ribosomes

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Summary

The proteins of E. coli ribosomes were separated by a specially developed type of preparative polyacrylamide gel electrophoresis and proteins corresponding to 16 of the separated bands have so far been isolated. The amino acid compositions and the tryptic peptide maps of these proteins show certain degree of similarity as well as distinct differences. Determination of molecular weights revealed a wide range: The lowest molecular weight was 9,000 and the highest 41,000 for the proteins so far studied.

The similarities between various ribosomal proteins in their amino acid compositions and their peptide maps on one hand and the wide range in their molecular weights on the other hand can be explained by a hypothesis involving gene duplications.

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Authors and Affiliations

  1. Max-Planck-Institut für Molekulare Genetik, Berlin-Dahlem

    E. Kaltschmidt, M. Dzionara, D. Donner & H. G. Wittmann

Authors
  1. E. Kaltschmidt
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  2. M. Dzionara
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  3. D. Donner
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  4. H. G. Wittmann
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Kaltschmidt, E., Dzionara, M., Donner, D. et al. Ribosomal proteins. Molec. Gen. Genetics 100, 364–373 (1967). https://doi.org/10.1007/BF00334063

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  • DOI: https://doi.org/10.1007/BF00334063

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