1887

Abstract

SUMMARY: The intra- and extracellular concentrations of a number of phosphorylated intermediary metabolites in were measured radiochemically during growth in low phosphate (0.75 mM) media containing [P]P. Distribution studies showed that most of the monophosphate metabolites were present in the supernatant medium outside the bacteria. This was much less marked for the di- and triphosphates, and was not due to bacterium lysis. Adenosine 3′,5′-cyclic monophosphate was present solely in the medium under all conditions tested. 3′,5′-Cyclic-AMP added to the medium was only partly effective in reversing repression of β-galactosidase synthesis by gluconate. This was not due to degradation of the nucleotide.

In another series of strains, chemical determinations were made of the intra-and extracellular concentrations of fructose 1,6-diphosphate and triose phosphate under varying conditions of growth in high phosphate (0·1 M) media; while most of the fructose 1,6-diphosphate remained inside the bacteria, triose phosphate was present largely in the medium. In all of these studies there was no correlation between the severity of catabolite repression and the concentrations of metabolites either inside the bacteria, or in the medium.

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/content/journal/micro/10.1099/00221287-71-1-181
1972-06-01
2021-10-23
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References

  1. Bucher T., Hohorst H. J. 1965 Dihydroxyacetone phosphate, fructose-i,6-diphosphate and D- glyceraldehyde-3-phosphate. Determination with glycerol-1-phosphate dehydrogenase, aldolase and triose phosphate dehydrogenase.. In Methods of Enzymatic Analysis , 2nd edn, pp 246–252 Edited by Bergmeyer H. U. New York and London:: Academic Press.;
    [Google Scholar]
  2. de Crombrugghe B., Perlman R. E., Varmus H. E., Pastan I. 1969; Regulation of inducible enzyme synthesis in Escherichia coli by cyclic adenosine 3′,5′-monophosphate.. Journal of Biological Chemistry 244:5828–5835
    [Google Scholar]
  3. Crowley G. J., Moses V., Ullrich J. 1963; A versatile solvent to replace phenol for the paper chromatography of radioactive intermediary metabolites.. Journal of Chromatography 12:219–228
    [Google Scholar]
  4. Lowry O. H., Rosebrough N. J., Farr A. L., Randall R. J. 1951; Protein measurement with the Folin phenol reagent.. Journal of Biological Chemistry 193:265–275
    [Google Scholar]
  5. Makman R. S., Sutherland E. W. 1965; Adenosine 3′,5′-phosphate in Escherichia coli.. Journal of Biological Chemistry 240:1309–1314
    [Google Scholar]
  6. Monod J. 1942 Recherches sur la croissance des cultures bacteriennes.. Paris:: Hermann.;
    [Google Scholar]
  7. Moses V., Lonberg-Holm K. K. 1963; A semi-automatic device for measuring radioactivity on twodimensional paper chromatograms.. Analytical Biochemistry 5:11–27
    [Google Scholar]
  8. Moses V., Prevost C. 1966; Catabolite repression of β-galactosidase synthesis in Escherichia coli.. Biochemical Journal 100:336–353
    [Google Scholar]
  9. Moses V., Sharp P. B. 1970; Adenosine 3′,5′-cyclic monophosphate and catabolite repression in Escherichia coli.. Biochemical Journal 118:481–489
    [Google Scholar]
  10. MOSES V., Wild D. G. 1969; Soluble protein profiles in Escherichia coli.. Folia microbiologica 14:305–309
    [Google Scholar]
  11. Okabayashi T., Ide M., Yoshimoto A. 1963; Excretion of adenosine-3′,5′-phosphate in the culture broth of Brevibacterium liquefaciens.. Archives of Biochemistry and Biophysics 100:158
    [Google Scholar]
  12. Okabayashi T., Yoshimoto A., Ide M. 1963; Occurrence of nucleotides in culture fluids of microorganisms. V. Excretion of adenosine cyclic 3′,5′-phosphate by Brevibacterium liquefaciens Sp. N.. Journal of Bacteriology 86:930–936
    [Google Scholar]
  13. Palmer J., Moses V. 1968; The role of the regulator-gene product (repressor) in catabolite repression of β-galactosidase synthesis in Escherichia coli.. Biochemical Journal 106:339–343
    [Google Scholar]
  14. Pardee A. B., Prestidge L. S. 1961; The initial kinetics of enzyme induction.. Biochimica et biophysica acta 49:77–88
    [Google Scholar]
  15. Porter J. R. 1946 Bacterial Chemistry and Physiology.. New York:: John Wiley.;
    [Google Scholar]
  16. Prevost C., Moses V. 1967; Pool sizes of metabolic intermediates and their relation to glucose repression of β-galactosidase synthesis in Escherichia coli.. Biochemical Journal 103:349–357
    [Google Scholar]
  17. Roberts R. B., Abelson P. H., Cowie D. B., Bolton E. T., Britten R. J. 1955 Studies of Biosynthesis in Escherichia coli.. Carnegie Institution Publication 607 Washington, D.C.:: Carnegie Institution.;
    [Google Scholar]
  18. Ruffilli D. 1933; Studies on the specific gravity of bacteria.. Biochemische Zeitschrift 263:63–74
    [Google Scholar]
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