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Superoxide dismutase activity in nematodes

Published online by Cambridge University Press:  05 June 2009

M. Sanchez-Moreno ,
P. Leon ,
M. A. Garcia-Ruiz  and
M. Monteoliva
M. Sanchez-Moreno
Affiliation:
Sección de Bioquímica, Instituto “López-Neyra” de Parasitología, C.S.I.C., C/Ventanilla 11, Granada 18001, Spain
P. Leon
Affiliation:
Sección de Bioquímica, Instituto “López-Neyra” de Parasitología, C.S.I.C., C/Ventanilla 11, Granada 18001, Spain
M. A. Garcia-Ruiz
Affiliation:
Sección de Bioquímica, Instituto “López-Neyra” de Parasitología, C.S.I.C., C/Ventanilla 11, Granada 18001, Spain
M. Monteoliva
Affiliation:
Sección de Bioquímica, Instituto “López-Neyra” de Parasitología, C.S.I.C., C/Ventanilla 11, Granada 18001, Spain
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Abstract

The activities of the enzymes superoxide dismutase (E.C.:1.15.1.1) and catalase (E.C: 1.11.1.6) were studied in purified extracts of four nematodes: Ascaris suum, Toxascaris leonina, Toxocara canis and T. cati adult males and females. No catalase activity was found in any of the extracts. The results reveal that the SOD activities of the four parasites presented species differences and also sexual differences within each species. Polyacrylamide gel electrophoresis pattern analysis confirmed that the mobilities, widths and band intensities varied according to the species and sex of the parasite from which the enzyme was obtained.

Keywords

Ascaris suumToxascaris leoninaToxocara canisToxocara catisuperoxide dismutaseelectrophoresisenzymescatalase

Information

Type
Research Papers
Information
Journal of Helminthology , Volume 61 , Issue 3 , September 1987 , pp. 229 - 232
Copyright
Copyright © Cambridge University Press 1987

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References

REFERENCES

Ayala, F. J., Powell, J. R., Tracey, M. L., Mourao, C. A. & Perez-Salas, F. (1972) Enzyme variability in the Drosophila willistom group. Genetics, 70, 113–139.CrossRefGoogle ScholarPubMed
Beers, R. F. & Sizer, I. V. (1952) A spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase. Journal of Biological Chemistry, 195, 133–140.CrossRefGoogle ScholarPubMed
Fehrnstrom, H. & Moberg, V. (1977) SDS and conventional polyacrylamide gel electrophoresis with LKB 2117 Multiphor. Application Note 306.Google Scholar
Garcia-Ruiz, M. A. & Monteoliva, M. & Sanchez-Moreno, M. (1986) Algunas aportaciones a la caracterización del enzima SOD en Moniezia expansa (Cestoda). Revista Iberica de Parasitologia, 45, 384–386.Google Scholar
Gerasimov, A. M., Kasatkina, N. V. & Darmova, E. N. (1979) Presence of antioxidant defense enzymes in the ascarid Ascaris lumbricoides. Journal of Evolutionary Biochemistry and Physiology, 15, 126–130.Google ScholarPubMed
Henry, L. E. A., Cammack, R., Schwitzguebel, J. P., Palmer, J. M. & Hall, D. O. (1980) Intracellular localization, isolation and characterization of two distinct varieties of superoxide dismutase from Neurospora crassa. Biochemical Journal, 187, 321–328.CrossRefGoogle ScholarPubMed
Hewitt, J. & Morris, J. G. (1975) Superoxide dismutase in some obligately anaerobic bacteria. FEBS Letters, 50, 315–318.CrossRefGoogle ScholarPubMed
Klebanoff, S. J. & Clark, R. A. (1978) The metabolic burst. In: The Neutrophil Function and Clinical Disorders, p. 290. Elsevier/North Holland: New York.Google Scholar
Lowry, O. H. & Rosebrough, N. J. & Farr, A. L. & Randall, R. J. (1951) Protein measurement with the Folin phenol reagent. Journal of Biological Chemistry, 193, 265–275.CrossRefGoogle ScholarPubMed
Mccord, J. M. & Fridovich, I. (1969) Superoxide dismutase: an enzymic function for erythro-cuprein (hemocuprein). Journal of Biological Chemistry, 244, 6049–6055.CrossRefGoogle ScholarPubMed
Mccord, J. M. & Keele, B. B. & Fridovich, I. (1971) An enzyme based theory of obligate anaerobiosis. The physiological function of superoxide dismutase. Proceedings of the National Academy of Sciences of the United States of America, 68, 1024–1027.CrossRefGoogle ScholarPubMed
Paul, J. M. & Barrett, J. (1980) Peroxide metabolism in the cestodes Hymenolepis diminuta and Moniezia expansa. International Journal for Parasitology, 10, 121–124.CrossRefGoogle Scholar
Poulik, M. D. (1957) Starch gel electrophoresis in a discontinuous system of buffers. Nature 180, 1477–1478.CrossRefGoogle Scholar
Rhoads, M. C. (1983) Trichinella spiralis: Identification and purification of superoxide dismutase. Experimental Parasitology, 56, 41–54.CrossRefGoogle ScholarPubMed