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The synthesis of β-galactosidase inEscherichia coli in the presence of 7-azatryptophan

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Abstract

The presence of 7-azatryptophan an analogue of tryptophan in the growth medium ofEscherichia coli resulted in a considerable inhibition of the synthesis of active β-galactosidase. No synthesis of an immunologically cross-reacting protein was detected. In addition, the replacement of tryptophan by the analogue rendered the enzyme more susceptible to heat, urea and trypsin as compared with the normal enzyme. The inhibition of growth and enzyme synthesis by 7-azatryptophan was reversed by tryptophan. The analogue did not exhibit any effect on the synthesis and activity of β-galactoside permease.

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Authors and Affiliations

  1. Department of General Microbiology, Institute of Microbiology, Czechoslovak Academy of Sciences, Prague 4

    J. Janeček & J. Spížek

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  1. J. Janeček
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  2. J. Spížek
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Janeček, J., Spížek, J. The synthesis of β-galactosidase inEscherichia coli in the presence of 7-azatryptophan. Folia Microbiol 14, 529–535 (1969). https://doi.org/10.1007/BF02884164

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  • DOI: https://doi.org/10.1007/BF02884164

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