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Some properties of l-chloro-2,4-dinitrochlorobenzene linked glutathione S-transferase in dichlorvos resistant and susceptible strains of cotton aphid (Homoptera: Aphididae)

Published online by Cambridge University Press:  27 March 2009

E. O. Owusu  and
M. Horiike
E. O. Owusu
Affiliation:
Department of Bioresources Science, Kochi University, B200 Monobe, Nankoku-shi, Kochi 783, Japan
M. Horiike
Affiliation:
Department of Bioresources Science, Kochi University, B200 Monobe, Nankoku-shi, Kochi 783, Japan
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Summary

Effects of temperature, hydrogen ion and substrate concentrations on conjugation of l-chloro-2,4-dinitrochlorobenzene by glutathione S-transferase from susceptible and dichlorvos-resistant strains of cotton aphid (Aphis gossypii Glover (Homoptera: Aphididae)) were evaluated. Enzymes from both strains had common optimum temperature and substrate concentration values of 30 °C and 10 mM respectively. Also, while enzyme activity of the susceptible strain peaked at pH 7·2, that of the resistant strain showed complete linear dependency up to pH 8·0. Of four subcellular fractions, the 100 000 g supernatant (soluble fraction) gave the highest enzyme activity in both phosphate and Tris/HCl buffers. There was no linear relationship between insecticide application frequency and production of enzyme activity in the susceptible strain but there was a very high positive correlation between these two parameters in the resistant strain.

Type
Crops and Soils
Information
The Journal of Agricultural Science , Volume 127 , Issue 4 , December 1996 , pp. 469 - 473
Copyright
Copyright © Cambridge University Press 1996

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References

REFERENCES

Balabaskaran, S., Chew, S. & Segaran, M. (1986). Studies on glutathione S-transferase in molluscs. Comparative Biochemistry and Physiology 85B, 183–192.Google Scholar
Booth, J., Boyland, E. & Sims, P. (1961). An enzyme from rat liver catalysing conjugations with glutathione. Biochemical Journal 79, 516–524.CrossRefGoogle ScholarPubMed
Boyland, E. & Chasseaud, L. F. (1967). Enzyme-catalysed conjugations of glutathione with unsaturated compounds. Biochemical Journal 104, 95–102.CrossRefGoogle ScholarPubMed
Egass, E., Svendsen, N. O., Kobro, S., Skaare, J. U. & Jensen, E. G. (1991). Activities and properties of xenobiotic metabolizing enzymes in the peach-potato aphid (Myzus persicae Sulzer) feeding on paprika (Capsicum annuum L.) or swedes (Brassica napus rapifera Metzger). Comparative Biochemistry and Physiology 99C, 105–110.Google Scholar
Habig, W. H., Pabst, M.J. & Jakoby, W. B. (1974). Glutathione S-transferases. The first enzymatic step in mercapturic acid formation. Journal of Biological Chemistry 249, 7130–7139.CrossRefGoogle ScholarPubMed
Hodgson, E. & Kulkarni, A. P. (1983). Characterization of cytochromc P-450 in studies of insecticide resistance. In Pesi Resistance to Pesticides (Eds Georghiou, G. P. & Saito, T.), pp. 207–228. New York: Plenum Press.CrossRefGoogle Scholar
Kao, C.-H., Hung, C.-F. & Sun, C.-N. (1989). Parathion and methyl parathion resistance in diamondback moth (Lepidoptera: Plutellidae) larvae. Journal of Economic Entomology 82 1299–1304.CrossRefGoogle Scholar
Motoyama, N. & Dauterman, W. C. (1977). Purification and properties of housefly glutathione S-transferase. Insect Biochemistry 7, 361–369.CrossRefGoogle Scholar
Motoyama, N. & Dauterman, W. C. (1980). Glutathione S-transferases: their role in the metabolism of organophosphorus insecticides. Review of Biochemical Toxicology 2, 49–69.Google Scholar
Motoyama, N., Rock, G. C. & Dauterman, W. C. (1971). Studies on the mechanism of azinphosmethyl resistance in the predaceous mite, Neoseiulus (T.) fallacis (Family: Phytoseiidae). Pesticide Biochemistry and Physiology 1, 205–215.Google Scholar
O'Brien, P. J., Abdel-Aal, Y. A., Ottea, J. A. & Graves, J. B. (1992). Relationship of insecticide resistance to carboxylesterase in Aphis gossypii (Homoptera: Aphididae) from Midsouth cotton. Journal of Economic Entomology 85, 651–657.CrossRefGoogle Scholar
Owusu, E. O., Komi, K., Horiike, M. & Hirano, C. (1994). Some properties of carboxylesterase from Aphis gossypii Glover (Homoptera: Aphididae). Applied Entomology and Zoology 29, 47–53.Google Scholar
Owusu, E. O., Horiike, M. & Hirano, C. (1996). Polyacrylamide gel electrophoretic assessments of some esterases in cotton aphid (Homoptera:Aphididae) resistance to dichlorvos. Journal of Economic Entomology 89, 302–306.CrossRefGoogle Scholar
Pabst, M. J., Habig, W. H. & Jakoby, W. B. (1974). Glutathione S-transferase A. A novel kinetic mechanism in which the major reaction pathway depends on substrate concentration. Journal of Biological Chemistry 249, 7140–7150.CrossRefGoogle ScholarPubMed
Shishido, T. & Fukami, J. (1963). Studies on the selective toxicities of organic phosphorus insecticides. (II). The degradation of the ethyl parathion, methyl parathion, and sumithion in mammal, insect and plant. Botyu-Kagaku 28, 69–76.Google Scholar
Terriere, L. C. (1983). Enzyme induction, gene amplification and insect resistance to insecticides. In Pest Resistance to Pesticides (Eds Georghiou, G. P. & Saito, T.), pp. 265–297. New York: Plenum Press.CrossRefGoogle Scholar
Yang, R. S. H., Hodgson, E. & Dauterman, W. C. (1971). Metabolism in vitro of diazinon and diazoxon in susceptible and resistant houseflies. Journal of Agricultural and Food Chemistry 19, 14–19.Google Scholar