Hostname: page-component-586b7cd67f-dlnhk Total loading time: 0 Render date: 2024-11-29T11:58:20.128Z Has data issue: false hasContentIssue false
  • English
  • Français

Kinetic and electrophoretic studies on acid and alkaline phosphatases of the metacercariae of Clinostomum complanatum (Trematoda: Digenea)

Published online by Cambridge University Press:  18 November 2009

Afzal A. Siddiqui  and
Wajih A. Nizami
Afzal A. Siddiqui
Affiliation:
Section of Parasitology, Department of Zoology, Aligarh Muslim University, Aligarh-202001, India
Wajih A. Nizami
Affiliation:
Section of Parasitology, Department of Zoology, Aligarh Muslim University, Aligarh-202001, India
Get access Rights & Permissions [Opens in a new window]

Abstract

Homogenates of the metacercariae of Clinostomum complanatum showed two peaks for the hydrolysis of p-nitrophenyl phosphate at pH 4·5–5·0 and 11·0; specific activity at pH 5·0 was 0·017 µmol p-nitrophenol/mg protein/min and 0·0049 µmol p-nitrophenol/mg protein/min at pH 11·0 at 37°C. Maximal activities of acid and alkaline phosphatases were observed at 50° and 40°C respectively. Both enzymes reached maximal rates after 50 min of incubation. Linearity in enzyme activity was noticed with increasing homogenate concentrations for both enzymes. The Km for p-nitrophenyl phosphate was 1·1 mM with a Vmax of 0·018 units/mg protein for acid phosphatase and 1·6 mM with a Vmax of 0·0052 units/mg protein for alkaline phosphatase. Sodium arsenate and sodium fluoride inhibit and Mg++ and Co++ stimulate both enzymes. Polyacrylamide gel electrophoresis showed one cathodic band each for both the enzymes.

Type
Research Papers
Information
Journal of Helminthology , Volume 56 , Issue 1 , March 1982 , pp. 17 - 22
Copyright
Copyright © Cambridge University Press 1982

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

Bergmeyer, H. U., Gawehn, K. & Grassl, M. (1974) Enzymes as biochemical reagents. In: Methods in Enzymatic Analysis. 2nd edit. (Bergmeyer, H. U., Editor) Vol. I, pp. 425–522. New York: Academic Press.Google Scholar
Boyer, S. H. (1961) Alkaline phosphatase in human sera and placentae. Science, 134, 1002.CrossRefGoogle ScholarPubMed
Cesari, I. M. (1974) Schistosoma monsoni: Distribution and characteristics of alkaline and acid phosphatase. Experimental Parasitology, 36, 405–414.CrossRefGoogle Scholar
Dennis, E. A., Sharp, M. & Douglass, R. (1974) Carbohydrate reserve and phosphatase activity in mollusc-trematode relationship of Mytilus edulis L and Proctoeces maculatus (Loos, 1901) Odhner, 1911. Journal of Helminthology, 48, 1–14.CrossRefGoogle Scholar
Erasmus, D. A. (1957) Studies on phosphatase system of cestodes. I. Studies on Taenia pisiformis (cysticercus and adult). Parasitology, 47, 70–80.CrossRefGoogle ScholarPubMed
Forster, R. & 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
Goil, M. M. (1973) Phosphatase system in Fasciolopsis buski Lankester, 1897 and Gastrodiscus aegyptiacus Cobbold, 1876. Parasitology, 50, 235–240.Google Scholar
Gupta, S. P. & Gupta, R. C. (1977) Phosphatase activity in Ganeo tigrinum from Rana tigrina. Zeitschrift für Parasitenkunde, 54, 89–94.CrossRefGoogle Scholar
Lowry, O. N., Rosebrough, N., Farr, A. & Randall, R. (1951) Protein measurement with Folin phenol reagent. Journal of Biological Chemistry, 193, 266–275.CrossRefGoogle ScholarPubMed
Ma, L. (1964) Acid phosphatase in Clonorchis sinensis. Journal of Parasitology, 50, 235–240.CrossRefGoogle ScholarPubMed
Nizami, W. A., Siddiqi, A. H. & Yusufi, A. N. K. (1975) Non-specific alkaline phosphomonoesterases of eight species of digenetic trematodes. Journal of Helminthology, 49, 281–287.CrossRefGoogle ScholarPubMed
Probert, A. J. & Lwin, T. (1974) Kinetic properties and location of non-specific phosphomonoesterases in the subcellular fractions of Fasciola hepatica. Experimental Parasitology, 35, 253–261.CrossRefGoogle Scholar
Probert, A. J. & Lwin, T. (1976) Fasciola hepatica: The presence of particle associated and soluble non-specific acid phosphatases. Experimental Parasitology, 40, 206–211.CrossRefGoogle Scholar
Sharma, P. N. (1976) Histochemical studies on the distribution of alkaline phosphatase, acid phosphatase, 5-nucleotidase and ATPase in the various reproductive tissues of certain digenetic trematodes. Zeitschrift für Parasitenkunde, 49, 223–231.CrossRefGoogle ScholarPubMed
Sur, B. K., Moss, D. W. & King, E. J. (1962) Starch-gel electrophoresis of prostatic acid phosphatase. Proceedings of the Association of Clinical Biochemists, 2, 11–13.CrossRefGoogle Scholar
Von Brand, T. (1973) Biochemistry of Parasites, 2nd edit. New York: Academic Press.Google Scholar