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Tricarboxylic acid cycle enzymes of a pseudophyllid cestode Penetrocephalus ganapatii

Published online by Cambridge University Press:  05 June 2009

S. Dhandayuthapani
Affiliation:
Department of Zoology, University of Madras, Guindy Campus, Madras – 600 025, India.
K. Nellaiappan
Affiliation:
Department of Zoology, University of Madras, Guindy Campus, Madras – 600 025, India.

Abstract

Studies on the tricarboxylic acid cycle (TCA cycle) enzymes of Penetrocephalus ganapatii reveal that the TCA cycle is only partially operative, as some of the enzymes at the start of the cycle viz. citrate synthase, aconitase and isocitrate dehydrogenase are found to be low in their activities. The high activities of malate dehydrogenase and fumarase, showing affinity towards a reverse direction, indicate that the TCA cycle operates in the reverse direction resulting in the formation of fumarate. The low succinate dehydrogenase/fumarate reductase ratio suggests that ATP generation may occur at site I of the respiratory chain during the reduction of fumarate into succinate.

Type
Research Note
Copyright
Copyright © Cambridge University Press 1990

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References

REFERENCES

Barrett, J. (1976) Bioenergetics in helminths. In: Biochemistry of parasites and host-parasite relationships (editor, Van Den Bossche, H.), pp. 6780. Elsevier, Amsterdam.Google Scholar
Barrett, J. (1981) Biochemistry of Parasitic Helminths. Macmillan, London.Google Scholar
Fioravanti, C.F. & Saz, H.J. (1976) Pyridine nucleotide transhydrogenases of parasitic helminths. Archives of Biochemistry and Biophysics, 175, 2130.Google Scholar
Kornberg, A. (1955) Isocitric dehydrogenase of yeast (DPN). In: Methods in Enzymology (editors, Colowick, S.P. and Kaplan, N.O.) Vol. I, pp. 707709, Academic Press, New York.CrossRefGoogle Scholar
KÖrting, W. (1976) Metabolism in parasitic helminths of freshwater fish. In: Biochemistry of parasites and host-parasite relationships (editor,Van Den Bossche, H.), pp. 95100, Elsevier, Amsterdam.Google Scholar
KÖrting, W. & Barrett, J. (1977) Carbohydrate catabolism in the plerocercoids of Schistocephalus solidus (Cestoda: Pseudophyllidea). International Journal for Parasitology, 7, 411417.CrossRefGoogle Scholar
Lowry, O.H., Rosebrough, N.H., Farr, A.L. & Randall, R.J. (1951) Protein measurement with the folin phenol reagent. The Journal of Biological Chemistry, 193, 265275.CrossRefGoogle ScholarPubMed
Massey, V. (1960) The composition of the ketoglutarate dehydrogenase complex. Biochimica et Biophysica Acta, 38, 447460.CrossRefGoogle ScholarPubMed
Mcmanus, D.P. (1975) Tricarboxylic acid cycle enzymes in the plerocercoid of Ligula intestinalis (Cestoda: Pseudophyllidea). Zeitschriftfür Parasitenkunde, 45, 319322.CrossRefGoogle ScholarPubMed
Mcmanus, D.P. & Smyth, J.D. (1982) Intermediary carbohydrate metabolism in protoscoleces of Echinococcus granulosus (horse and sheep strains) and E. multilocularis. Parasitology, 84, 351366.CrossRefGoogle ScholarPubMed
Ochoa, S. (1955) Crystalline condensing enzyme from pig heart. In: Methods in Enzymology (editors, Colowick, S.P. and Kaplan, ) Vol. I, pp. 685694. Academic Press, New York.CrossRefGoogle Scholar
Pappas, P.W. & Schroeder, L.L. (1979) Hymenolepis microstoma: Lactate and malate dehydrogenases of the adult worm. Experimental Parasitology, 47, 134139.CrossRefGoogle ScholarPubMed
Plaut, W.E. & Sung, S.C. (1955) Diphosphopyridine nucleotide isocitric dehydrogenase from animal tissues. In: Methods in Enzymology (editors, Colowick, S.P. and Kaplan, N.O.) Vol. I. pp. 710714, Academic Press, New York.Google Scholar
Racker, E. (1950) Spectrophotometric measurement of the enzymatic formation of fumaric and cis-aconitic acids. Biochimica et Biophysica Acta, 4, 211214.CrossRefGoogle ScholarPubMed
Ribeiro, L.P., Ferreira, M.F.A. & Andrade, C.M. (1981) Compartmentalization and one step preparation of enzymes of malate metabolism in muscle extracts of Toxocara canis. Comparative Biochemistry and Physiology, 68B, 859864.Google Scholar
Sanadi, D.R. & Fluharty, A.L. (1963) On the mechanism of oxidative phosphorylation VII. The energy requiring reduction of pyridine nucleotide by succinate and the energy-yielding oxidation of reduced pyridine nucleotide by fumarate. Biochemistry, 2, 523528.Google Scholar
Singer, T.P. (1974) Determination of the activity of succinate, NADH, choline and α-glycerophosphate dehydrogenase. In: Methods in Biochemical Analysis (editor Glick, D.), Vol. 22, pp. 133140. Interscience publication, John Wiley and Sons, New York.Google Scholar
Yoshida, A. (1969) L-malate dehydrogenase from Bacillus subtilis. In: Methods in Enzymology (editor Lowenstein, J.M.) Vol. XIII, pp. 141145. Academic Press, New York.Google Scholar