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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
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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

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References

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