Hostname: page-component-586b7cd67f-r5fsc Total loading time: 0 Render date: 2024-11-23T06:30:43.806Z Has data issue: false hasContentIssue false
  • English
  • Français

Activation of succinate dehydrogenase from adult Fasciola hepatica (Trematoda)

Published online by Cambridge University Press:  06 April 2009

J. Barrett
J. Barrett
Affiliation:
Department of Zoology, University College of Wales, Aberystwyth, Dyfed SY23 3DA
Get access Rights & Permissions [Opens in a new window]

Summary

The succinate dehydrogenase of adult Fasciola hepatica was found to exist in active and inactive forms. The enzyme was inactivated by 1 μM oxaloacetate and activated by incubation with compounds which bind to the active site (succinate, fumarate, malonate) or by incubation with anions and certain nucleotides. The activation of the enzyme by succinate followed first-order kinetics. The extent of activation of F. hepatica succinate dehydrogenase depended on the nature and concentration of the activator and on the pH. The rate of activation of the enzyme depended on the temperature. In contrast, the fumarate reductase activity of F. hepatica was not activated by incubation with substrate or anions and was not inhibited by oxaloacetate (100 μM). The significance of these results in the regulation of the tricarboxylic acid cycle in parasitic helminths is discussed.

Type
Research Article
Information
Parasitology , Volume 76 , Issue 3 , June 1978 , pp. 269 - 275
Copyright
Copyright © Cambridge University Press 1978

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

Ackrell, B. A. C., Kearney, E. B. & Mayr, M. (1974). Role of oxalacetate in the regulation of mammalian succinate dehydrogenase. Journal of Biological Chemistry 249, 2021–7.CrossRefGoogle ScholarPubMed
Barrett, J. (1976). Bioenergetics in helminths. In Biochemistry of Parasites and Host-Parasite Relationships (ed. Van den Bossche, H.), pp. 67–80. Amsterdam: Elsevier.Google Scholar
Coles, G. C. (1975). Fluke biochemistry – Fasciola and Schistosoma. Helminthological Abstracts A 44, 147–62.Google Scholar
Dawes, B. (1954). Maintenance in vitro of Fasciola hepatica. Nature, London 174, 654–5.CrossRefGoogle ScholarPubMed
Gutman, M. (1976). The effect of opposing effectors on activation level of succinate de. hydrogenase: equilibrium and kinetic studies. Biochemistry 15, 1342–8.CrossRefGoogle Scholar
Kearney, E. B., Ackrell, B. A. C., Mayr, M. & Singer, T. P. (1974). Activation of succinate dehydrogenase by anions and pH. Journal of Biological Chemistry 249, 2016–20.CrossRefGoogle ScholarPubMed
Kimura, T., Hauber, J. & Singer, T. P. (1967). Studies on succinate dehydrogenase 13. Reversible activation of the mammalian enzyme. Journal of Biological Chemistry 242, 4987–93.CrossRefGoogle ScholarPubMed
Körting, W. & Barrett, J. (1977). Carbohydrate catabolism in the plerocercoids of Schistocephalus solidus (Cestoda: Pseudophyllidea). International Journal for Parasitology 7, 411–17.CrossRefGoogle Scholar
Lara, F. J. S. (1959). The succinic dehydrogenase of Propionibacterium pentosaceum. Biochimica et Biophysica Acta 33, 565–7.CrossRefGoogle ScholarPubMed
Metzger, H. & Düwel, D. (1973). Investigations of metabolism in the liver fluke (Fasciola hepatica) as an aid to the development of new anthelmintics. International Journal of Biochemistry 4, 133–43.CrossRefGoogle Scholar
Podesta, R. B., Mustafa, T., Moon, T. W., Hulbert, W. C. & Mettrick, D. F. (1976). Anaerobes in an aerobic environment: role of CO2 in energy metabolism of Hymenolepis diminuta. In Biochemistry of Parasites and Host-Parasite Relationships (ed. Van den Bossche, H.), pp. 81–8. Amsterdam: Elsevier.Google Scholar
Prichard, R. K. (1973). The fumarate reductase reaction of Haemonchus contortus and the mode of action of some anthelmintics. International Journal for Parasitology 3, 409–17.CrossRefGoogle ScholarPubMed
Singer, T. P., Kearney, E. B. & Gutman, M. (1972). Regulation of succinic dehydrogenase in mitochondria. In Biochemical Regulatory Mechanisms in Eukaryotic Cells (ed. Kun, E. and Grisolia, S.), pp. 271–301. New York: Wiley.Google Scholar
Singer, T. P., Kearney, E. B. & Kenney, W. C. (1973). Succinate dehydrogenase. Advances in Enzymology 37, 189–272.Google ScholarPubMed
Thorn, M. B. (1962). Activation of succinate dehydrogenase in heart-muscle preparations. Biochemical Journal 85, 116–27.CrossRefGoogle ScholarPubMed
Van den Bossche, H. (1972). Studies on phosphorylation in Ascaris mitochondria. In Comparative Biochemistry of Parasites (ed. Van den Bossche, H.), pp. 455–68. New York: Academic Press.CrossRefGoogle Scholar
Warringa, M. G. P. J., Smith, O. H., Guiditta, A. & Singer, T. P. (1958). Studies on succinic dehydrogenase 8. Isolation of a succinic dehydrogenase – fumaric reductase from an obligate anaerobe. Journal of Biological Chemistry 230, 97–109.CrossRefGoogle Scholar