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Molecular and General Genetics MGG

, Volume 109, Issue 4, pp 303–308 | Cite as

Ribosomal proteins

XVII. Comparative studies on ribosomal proteins of four strains ofEscherichia coli
  • E. Kaltschmidt
  • G. Stöffler
  • M. Dzionara
  • H. G. Wittmann
Article

Summary

The ribosomal proteins fromE. coli strains B, C, K12 (A19), and MRE600 were extracted and analyzed by two-dimensional polyacrylamide gel electrophoresis. All four strains were found to be indistinguishable in their 50S ribosomal protein components, while there were differences among the 30S proteins. Strains K and B differ in protein S5 and S7. Strain C differs from strain B in protein S5 and from strain K in protein S7. MRE600 appears to be identical to strain C in respect to its ribosomal protein pattern. It was furthermore found that proteins S7 from strain K and B differ extensively in respect to size, charge, amino acid composition and immunological properties. The rather remote relationship between these two analogous proteins is quite remarkable when contrasted with the striking similarity in all but one of the other 30S and 50S proteins of the strains.

Keywords

Electrophoresis Acid Composition Polyacrylamide Ribosomal Protein Amino Acid Composition 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer-Verlag 1970

Authors and Affiliations

  • E. Kaltschmidt
    • 1
  • G. Stöffler
    • 1
  • M. Dzionara
    • 1
  • H. G. Wittmann
    • 1
  1. 1.Max-Planck-Institut für Molekulare GenetikBerlin-DahlemGermany

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