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Folia Microbiologica

, Volume 17, Issue 2, pp 143–150 | Cite as

The synthesis of β-galactosidase inEscherichia coli in the presence of Methionine analogues

  • J. Spížek
  • Z. Techniková
  • J. Beneš
  • J. Janeček
Article
  • 14 Downloads

Abstract

The effect of methionine analogues, selenomethionine and selenoethionine, on the synthesis of β-galactosidase inEscherichia coli was investigated. It was found that the incorporation of selenomethionine into β-galactosidase results in the formation of a protein exhibiting normal enzyme activity and immunologically cross-reacting with the antiserum against normal β-galactosidase. However, the selenomethionine enzyme was found to be more susceptible to heat, urea and trypsin. On the other hand, an immunologically cross-reacting protein without the enzyme activity was synthesized in the presence of selenoethionine. The results obtained seem to support the idea that the presence of methionine methyl groups is essential for the activity of β-galactosidase, whereas methionine sulphur can be replaced without changing the enzyme activity.

Keywords

Methionine Selenomethionine Ethionine Immunological Test Bacterial Extract 
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

© Institute of Microbiology, Academy of Sciences of the Czech Republic 1972

Authors and Affiliations

  • J. Spížek
    • 1
  • Z. Techniková
    • 1
  • J. Beneš
    • 1
  • J. Janeček
    • 1
  1. 1.Department of General Microbiology, Institute of Microbiology and Isotope Laboratory of Biological InstitutesCzechoslovak Academy of SciencesPrague 4

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