Hostname: page-component-cd9895bd7-7cvxr Total loading time: 0 Render date: 2024-12-26T01:10:05.221Z Has data issue: false hasContentIssue false

Properties and localization of chitin synthase in Ascaris suum eggs

Published online by Cambridge University Press:  06 April 2009

P. Dubinský
Affiliation:
Helminthological Institute, Slovak Academy of Sciences, Dukelských hrdinov 3, 040 01 Košice, Czechoslovakia
M. Ryboš
Affiliation:
Helminthological Institute, Slovak Academy of Sciences, Dukelských hrdinov 3, 040 01 Košice, Czechoslovakia
Ľ. Turčeková
Affiliation:
Helminthological Institute, Slovak Academy of Sciences, Dukelských hrdinov 3, 040 01 Košice, Czechoslovakia

Summary

Investigations were carried out into the properties and localization of chitin synthase (EC 2.4.1.16) in connection with the formation of Ascaris suum egg-shells. The chitin synthase of eggs exhibited properties very similar to those found in other chitin-synthesizing organisms. It was stimulated by the presence of ATP, GlcNAc and Mg2+ with maximal activity at pH 7·0. In the phase of active chitin synthesis, during formation of the primary shell layers, chitin synthase was bound to the structures of the eggs. On completion of chitin synthesis in the eggs, the amount of the enzyme increased in the soluble fraction. Two forms of chitin synthase have been found in the eggs, namely an inactive (zymogenic) and an active form. Transformation of these two enzyme forms represents a key mechanism in the regulation of chitin synthesis in A. suum eggs.

Type
Research Article
Copyright
Copyright © Cambridge University Press 1986

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

REFERENCES

Arroyo-Begovich, A. & Ruiz-Herrera, J. (1979). Proteolytic activation and inactivation of chitin synthase from Neurospora crassa. Journal of General Microbiology 113, 339–45.CrossRefGoogle Scholar
Cabib, E., Ulane, R. & Bowers, B. (1973). Yeast chitin synthetase. Separation of the zymogen from its activating factor and recovery of the latter in the vacuole fraction. Journal of Biological Chemistry 248, 1451–8.CrossRefGoogle ScholarPubMed
Carey, F. G. (1965). Chitin synthesis in vitro by crustacean enzymes. Comparative Biochemistry and Physiology 16, 155–8.Google Scholar
Fähnrich, M. & Ahlers, J. (1981). Improved assay mechanism of the reaction catalysed by the chitin synthase from Saccharomyces cerevisiae. European Journal of Biochemistry 121, 113–18.Google Scholar
Foor, W. E. (1967). Ultrastructural aspects of oocyte development and shell formation in Ascaris lumbricoides. Journal of Parasitology 53, 1245–61.Google Scholar
Foor, W. E. (1968). Zygote formation in Ascaris lumbricoides (Nematoda). Journal of Cell Biology 39, 119–34.Google Scholar
Ghebregzabher, M., Rufini, S., Monaldi, B. & Lato, M. (1976). Thin-layer chromatography of carbohydrates. Journal of Chromatography 127, 113–62.CrossRefGoogle ScholarPubMed
Glaser, L. & Brown, D. H. (1957). The synthesis of chitin in cell-free extracts of Neurospora crassa. Journal of Biological Chemistry 228, 729–42.Google Scholar
Hohnke, L. A. (1971). Enzymes of chitin metabolism in the decapod, Hemigrapsusnudus. Comparative Biochemistry and Physiology 40B, 757–79.Google Scholar
Jan, Y. N. (1974). Properties and cellular localization of chitin synthetase in Phycomyces blakesleanus. Journal of Biological Chemistry 249, 1973–9.Google Scholar
Jaworski, E., Wang, L. & Marco, G. (1963). Synthesis of chitin in cell-free extracts of Prodenia eridania. Nature, London 198, 790.CrossRefGoogle Scholar
Kaulenas, M. S. & Fairbairn, D. (1968). RNA metabolism of fertilized Ascaris lumbricoides eggs during uterine development. Experimental Cell Research 52, 233–51.Google Scholar
Keller, F. A. & Cabib, E. (1971). Chitin and yeast budding: properties of chitin synthetase from Saccharomyces carlsbergensis. Journal of Biological Chemistry 246, 160–6.CrossRefGoogle ScholarPubMed
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, 165–75.CrossRefGoogle ScholarPubMed
Peberdy, J. F. & Moore, P. M. (1975). Chitin synthase in Mortierella vinacea: properties, cellular location and synthesis in growing cultures. Journal of General Microbiology 90, 228–36.CrossRefGoogle ScholarPubMed
Ruiz-Herrera, J., Sing, V. O., Van Der Woude, W. J. & Bartnicki-Garcia, S. (1975). Microfibril assembly by granules of chitin synthetase. Proceedings of the National Academy of Sciences, USA 72, 2706–10.CrossRefGoogle ScholarPubMed
Ryder, N. S. & Peberdy, J. F. (1977). Chitin synthase in Aspergillus nidulans: properties and proteolytic activation. Journal of General Microbiology 99, 6976.Google Scholar
Ulane, R. E. & Cabib, E. (1976). The activating system of chitin synthetase from Saccharomyces cerevisiae. Purification and properties of the activing factor. Journal of Biological Chemistry 251, 3367–74.Google Scholar