1887

Abstract

The content of glycogen phosphorylase (1,4-α--glucan:orthophosphate α--glucosyl-transferase, EC 2.4.1.1) in yeast () cells depended on the growth phase. Cells of the early exponential phase under carbohydrate-limited conditions showed low, but significant, phosphorylase activity; the activity markedly increased in the late exponential growth phase, concomitant with the appearance of measurable phosphorylase antigen. This pointed to an induction of the enzyme. During the interexponential phase (the slow proliferation phase during the diauxic growth of the culture, when the cells switch to utilization of accumulated ethanol) and the stationary growth phase, phosphorylase concentration remained constant while its specific molecular activity increased further, probably caused by conversion of the enzyme to an active form. During transition of stationary phase cells to growth, phosphorylase activity and concentration slowly decreased in the cells at a rate compatible with dilution by newly synthesized proteins. A residual activity always remained, which could be attributed to the presence of active phosphorylase, detectable by activity staining after gel electrophoresis in the presence of glycogen. No direct correlation could be detected between the specific molecular activity of phosphorylase and glycogen metabolism. This indicated that covalent modification of the enzyme regulated the total capacity of the enzyme available to the cell, rather than the actual activity limiting glycogen breakdown.

Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-128-3-447
1982-03-01
2021-08-01
Loading full text...

Full text loading...

/deliver/fulltext/micro/128/3/mic-128-3-447.html?itemId=/content/journal/micro/10.1099/00221287-128-3-447&mimeType=html&fmt=ahah

References

  1. Becker J. U. 1977; Glycogen synthase in Saccharomyces carlsbergensis cells capable of oscillatory glycolysis. Archives of Microbiology 115:181–184
    [Google Scholar]
  2. Becker J. U. 1979; Isolation and characterisation of an acid phosphatase interfering with phosphorylase determinations in crude extracts from yeast. Archives of Microbiology 123:233–238
    [Google Scholar]
  3. Becker J. U., Vohmann H. J., Eilers-König CHR. 1979; Glycogen metabolism in resting and growing cells of Saccharomyces carlsbergensis. Archives of Microbiology 123:143–149
    [Google Scholar]
  4. Cohen P.editor 1980; Recently discovered systems of enzyme regulation by reversible phosphorylation. Amsterdam: Elsevier-North Holland;
    [Google Scholar]
  5. Davis C. H., Schliselfeld L. D., Wolf D. P., Leavitt C. A., Krebs E. G. 1967; Interrelationships among glycogen phosphorylase isozymes. Journal of Biological Chemistry 242:4824–4833
    [Google Scholar]
  6. Fosset M., Muir L. W., Nielsen L. D., Fischer E. H. 1971; Purification and properties of yeast phosphorylase a and b. Biochemistry 10:4105–4113
    [Google Scholar]
  7. Gornall A. G., Bradawill C. J., David M. M. 1949; Determination of serum proteins by means of the biuret reaction. Journal of Biological Chemistry 177:751–766
    [Google Scholar]
  8. Helmreich E., Cori C. F. 1965; Regulation of glycolysis in muscle. Advances in Enzyme Regulation 3:91–107
    [Google Scholar]
  9. Holzer H. 1976; Catabolite inactivation in yeast. Trends in Biochemical Sciences 1:178–181
    [Google Scholar]
  10. Laurell C. B. 1966; Quantitative estimation of proteins by electrophoresis in agarose gels containing antibodies. Analytical Biochemistry 15:45–53
    [Google Scholar]
  11. Rothman-Denes L. B., Cabib E. 1970; Two forms of yeast glycogen synthetase and their role in glycogen accumulation. Proceedings of the National Academy of Sciences of the United States of America 66:967–974
    [Google Scholar]
  12. Schimke R. T. 1975; On the properties and mechanism of protein turnover. In Intracellular Protein Turnover pp. 173–186 Edited by Schimke R. T., Katunuma N. New York: Academic Press;
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-128-3-447
Loading
/content/journal/micro/10.1099/00221287-128-3-447
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