1887

Abstract

SUMMARY: 216 was induced with -galactose to form galactokinase (EC 2.7.1.6) in amounts comparable with those induced in K12. When compared with the basal level, the increase was 20 times greater than in

The greater the concentration of -galactose, the greater the production of galactokinase in both protoplasts and whole bacteria. In each case the maximum amount of enzyme was induced by 5 m -galactose. -Fucose, a gratuitous inducer, produced approximately half the specific activity of enzyme in protoplasts as -galactose at any particular concentration. The yield of enzyme in the presence of an optimal concentration of -galactose was increased when the medium was fortified with low concentrations of casein hydrolysate. The specific activities of galactokinase induced in protoplasts and in whole bacteria were respectively 148 % and 37 % greater in the presence of 0·01 % casein hydrolysate.

The maximum specific activity of galactokinase achieved after induction of protoplasts for 60 min. was 3·7 units/mg. protein compared with 12·5 units/ mg. protein in whole bacteria. However, over the first 15 min. after the addition of inducer the same specific activity of galactokinase was achieved in protoplasts as in whole bacteria.

Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-63-2-227
1970-10-01
2024-04-25
Loading full text...

Full text loading...

/deliver/fulltext/micro/63/2/mic-63-2-227.html?itemId=/content/journal/micro/10.1099/00221287-63-2-227&mimeType=html&fmt=ahah

References

  1. Bürgi W., Richterich R., Briner M. 1967; Ultraviolet photometric determination of total cerebrospinal fluid proteins with a modified biuret reagent. Clinica Chimica Acta 15:181–184
    [Google Scholar]
  2. Buttin G. 1963; Mécanismes régulateurs dans la biosynthèse des enzymes du métabolisme du galactose chez Escherichia coli k12. I. La biosynthese induite de la galactokinase et l’induction simultanée de la séquence enzymatique. Journal of Molecular Biology 7:164–182
    [Google Scholar]
  3. Buttin G. 1968; Les systèmes enzymatiques inductibles du métabolisme des oses chez Escherichia coli . In Advances in Enzymology 30: pp 81–137 Nord F. F. Edited by New York: Interscience;
    [Google Scholar]
  4. Coleman G., Elliott W. 1962; Studies on a-amylase formation by Bacillus subtilis . Biochemical Journal 83:256–263
    [Google Scholar]
  5. Coleman G., Elliott W. H. 1965; Extracellular ribonucléase formation in Bacillus subtilis and its stimulation by actinomycin D. Biochemical Journal 95:699–706
    [Google Scholar]
  6. Gulbinsky S., Cleland W. W. 1968; Kinetic studies of Escherichia coli galactokinase. Bio-chemistry 7:566–575
    [Google Scholar]
  7. Kiho Y., Rich A. 1964; Induced enzyme formed on bacterial polyribosomes. Proceedings of the National Academy of Sciences of the United States of America 51:111–118
    [Google Scholar]
  8. Landman O. E., Spiegelman S. 1955; Enzyme formation in protoplasts of Bacillus megaterium . Proceedings of the National Academy of Sciences of the United States of America 41:689–704
    [Google Scholar]
  9. Layne E. 1957; Spectrophotometric and turbidimetric methods for measuring proteins. In Methods in Enzymology 3 pp 447–454 Colowick S. P., Kaplan N. O. Edited by New York: Academic Press;
    [Google Scholar]
  10. Mcquillen K. 1955; Protein, nucleic acid and adaptive enzyme formation in protoplasts of Bacillus megaterium . Journal of General Microbiology 13:iv
    [Google Scholar]
  11. McQuillen K. 1960; Bacterial protoplasts. . In The Bacteria 1: pp. 249–359
    [Google Scholar]
  12. Paigen K. 1963; Changes in the inducibility of galactokinase and β-galactosidase during inhibition of growth in Escherichia coli . Biochimica et Biophysica Acta 77:318–328
    [Google Scholar]
  13. Sherman J. R., Adler J. 1963; Galactokinase from Escherichia coli . Journal of Biological Chemistry 238:873–878
    [Google Scholar]
  14. Wiame J. M., Storck R., Vanderwinkel E. 1955; Biosynthese induite d’arabinokinase dans les protoplastes de Bacillus subtilis . Biochimica et Biophysica Acta 18:353–357
    [Google Scholar]
  15. Wilson D. B., Hogness D. S. 1969; The enzymes of the galactose operon in Escherichia coli. IV. The frequencies of translation of the terminal cistron in the operon. Journal of Biological Chemistry 244:2143–2148
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-63-2-227
Loading
/content/journal/micro/10.1099/00221287-63-2-227
Loading

Data & Media loading...

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error