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Non-specific alkaline phosphomonoesterases of eight species of digenetic trematodes

Published online by Cambridge University Press:  05 June 2009

Wajih A. Nizami ,
Ather H. Siddiqi  and
A. N. K. Yusufi
Wajih A. Nizami
Affiliation:
Section of Parasitology, Department of Zoology, Aligarh Muslim University, Aligarh-202001, India
Ather H. Siddiqi
Affiliation:
Section of Parasitology, Department of Zoology, Aligarh Muslim University, Aligarh-202001, India
A. N. K. Yusufi
Affiliation:
Section of Parasitology, Department of Zoology, Aligarh Muslim University, Aligarh-202001, India
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Abstract

Alkaline phosphatases from different trematodes occupying the same habitat have identical pH optima but different levels of enzyme activities. Isoparorchis hypselobagri, from the fish Wallago attu, shows four to six times more enzyme activity than Fasciolopsis buski, Gastrodiscoides hominis and Echinostoma malayanum, from the pig Sus scrofa, and Fasciola gigantica, Gigantocotyle explanatum, Cotylophoron cotylophorum and Gastrothylax crumenifer, from the buffalo Bubalus bubalis.

At least two peaks of activity at different levels of pH were obtained for each trematode examined. Both Gastrodiscoides hominis and Isoparorchis hypselobagri enzymes had three peaks of alkaline phosphatase activity.

The optimum temperature for maximum enzyme activity was 40°C, above which rapid inactivation occurred. At temperatures below 40°C, the enzymes of fish and mammalian trematodes did not behave similarly; I. hypselobagri enzyme being active over a wider range of temperature (20°–40°C.

Various concentrations of KCN and arsenate proportionately inhibited enzyme activity. NaF did not significantly influence enzyme activity, while Mg++ and CO++ acted as activators. The extent of inhibition or activation of enzyme activity of different trematodes varied, probably due to species differences. Both inhibition and activation of I. hypselobagri enzyme was higher than in the case of other trematodes.

Type
Research papers
Information
Journal of Helminthology , Volume 49 , Issue 4 , December 1975 , pp. 281 - 287
Copyright
Copyright © Cambridge University Press 1975

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References

REFERENCE

Bartlett, G.R. (1959) Phosphorus assay in chromatography. Journal of Biological Chemistry, 234, 466–468.CrossRefGoogle ScholarPubMed
Von brand, T. (1973) Biochemistry of Parasites, p. pl8–21. Academic Press: New York.Google Scholar
Forster, R. and Taggart, T. (1950) Use of isolated renal tubules for the examination of metabolic processes associated with active cellular transport. Journal of Cellular and Comparative Physiology, 30, 251–270.CrossRefGoogle Scholar
Halton, D.W. (1967) Studies on phosphatase activity in Trematoda. Journal of Parasitology, 53, 46–54.CrossRefGoogle ScholarPubMed
Hawk, P.W., Oser, B.L. and Summerson, W.H. (1954) Practical Physiological Chemistry, pp 1118–1121. McGraw-Hill Book Company: New York.Google Scholar
Lowry, O., Roserbrough, N., Farr, A. and Randall, R. (1951) Protein measurements with the Folin phenol reagent. Journal of Biological Chemistry, 193, 266–275.CrossRefGoogle ScholarPubMed
Probert, A.J., Goil, M. and Sharma, R.K. (1972) Biochemical and histochemical studies on the non-specific phosphomonoesterase of Fasciola gigantica Cobbold, 1855. Parasitology, 64, 347–353.CrossRefGoogle ScholarPubMed
Probert, A.J. and Lwin, T. (1974) Kinetic properties and location of non-specific phosphomonoesterases in subcellular fractions of Fasciola hepatica. Experimental Parasitology, 35, 253–261.CrossRefGoogle Scholar
Roche, J. (1950) Phosphatases. In The Enzyme (ed J. B. Summer and K. Myrbach). Vol. I. pp 473–510. Academic Press: New York.Google Scholar