1887

Abstract

SUMMARY: Chondroitinase was induced in by chondroitin sulphate or by -acetylgalactosamine. With batch cultures growing on chondroitin sulphate or -acetylgalactosamine the differential rate of chondroitinase synthesis increased throughout the exponential growth phase. Induction of chondroitinase by chondroitin sulphate was prevented by glucose, glycerol, lactate, pyruvate or succinate. The rate of uptake of chondroitin sulphate by suspensions was not altered by the presence of glucose. With steady state chemostat cultures, limited either by the supply of chondroitin sulphate or nicotinic acid, the specific activity of chondroitinase was maximal at diffusion coefficient () = 0·18h. Addition of glucose to nicotinic acid-limited chemostat cultures resulted in an exponential reduction in chondroitinase specific activity; this could be partially prevented by the simultaneous addition of 5 m-adenosine cyclic-3′,5′-monophosphate.

Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-80-2-515
1974-02-01
2021-08-05
Loading full text...

Full text loading...

/deliver/fulltext/micro/80/2/mic-80-2-515.html?itemId=/content/journal/micro/10.1099/00221287-80-2-515&mimeType=html&fmt=ahah

References

  1. Clarke P. H., Houldsworth M. A., Lilly M. D. 1968; Catabolite repression and the induction of amidase synthesis by Pseudomonas aeruginosa 8602 in continuous culture. Journal of General Microbiology 51:225–234
    [Google Scholar]
  2. De Crombrugghe B., Perlman R. L., Varmus H. E., Pastan I. 1969; Regulation of inducible enzyme synthesis in Escherichia coli by cyclic-3′5′-adenosine monophosphate. Journal of Biological Chemistry 244:5828–5833
    [Google Scholar]
  3. Dean A. C. R. 1972; Influence of environment on the control of enzyme synthesis. Journal of Applied Chemistry and Biotechnology 22:245–259
    [Google Scholar]
  4. Dodgson K. S., Lloyd A. G. 1957; Study on sulphatases. XVIII. Preparation of chondroitinase-free chondrosulphatase from extracts of Proteus vulgaris . Biochemical Journal 66:532–539
    [Google Scholar]
  5. Hascall V. C., Riolo R. Z., Hayward J., Reynolds C. C. 1972; Treatment of bovine nasal cartilage proteoglycan with chondroitinases from Flavobacterium heparinum and Proteus vulgaris . Journal of Biological Chemistry 247:4521–4528
    [Google Scholar]
  6. Jobe A., Bourgeois S. 1972; lac Repressor-operator interaction. VI. The natural inducer of the lac operon. Journal of Molecular Biology 69:397–408
    [Google Scholar]
  7. Kempson G. E., Muir H., Pollard C., Tuke M. 1973; The tensile properties of the cartilage of human femoral condyles related to the content of collagen and glycosaminoglycans. Biochimica et biophysica acta 297:456–472
    [Google Scholar]
  8. 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]
  9. Martinez R. J., Wolfe J. B., Nakada H. I. 1959; Degradation of chondroitin sulphateby Proteus vulgaris . Journal of Bacteriology 78:217–224
    [Google Scholar]
  10. Mayes J. S., Hansen R. G. 1965; An enzymatic method for the determination of chondroitin sulphates. Analytical Biochemistry 10:15–22
    [Google Scholar]
  11. McFall E., Bloom F. 1971; Catabolite repression in the D-serine deaminase system of Escherichia coli K-12. Journal of Bacteriology 105:241–248
    [Google Scholar]
  12. Yamagata T., Saito H., Habuchi O., Suzuji S. 1968; Purification and properties of bacterial chondroitinases and chondrosulphatases. Journal of Biological Chemistry 243:1523–1535
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-80-2-515
Loading
/content/journal/micro/10.1099/00221287-80-2-515
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