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Effect of methionine on longevity, antioxygenic enzymes and lipid peroxides in Callosobruchus maculatus F.
Published online by Cambridge University Press: 19 September 2011
Abstract
The effect of methionine on longevity, antioxygenic enzymes and lipid peroxides in Callosobruchus maculatus was investigated using C. maculatus maintained on Vigna radiata seeds soaked in seven levels of methionine, 0, 1, 3, 5, 7, 9 and 12 mg/ml water. The life span and activities of catalase and peroxidase were higher in Callosobruchus maculatus infesting Vigna radiata seeds soaked in methionine as compared to their control cohorts. However, the lipid peroxide (malondialdehyde; MDA) levels generally remained unaltered. The present observation on the increased longevity in C. maculatus with methionine level is an extension of earlier findings on its anti-ageing effect in higher animals.
Résumé
L'effet de la méthionine sur la longevité, les enzymes antioxygéniques et les péroxydes de lipide chez Callosobruchus maculatus a été étudié sur C. maculatus cultivé sur de la graine de Vigna radiata. La graine a été trempée dans de la méthionine à 7 concentrations, à savoir 0, 1, 3, 5, 7, 9 et 12 mg de méthionine par ml d'eau. La durée de vie et les activités du catalase et du peroxidase ches Callosobruchus maculatus infestant les graines de Vigna radiata trempées dans la méthionine ont été supérieures, comparées aux cohortes témoins. Cependant, les niveaux du peroxide de lipide (malondialdehyde, MDA) étaient restés générallement inchangés. La présente observation sur la longevité accrue de C. maculatus avec le méthionine ajoute aux trouvailles antérieures sur son effet anti-vieillisement chez les animaux supérieures.
Keywords
- Type
- Research Articles
- Information
- International Journal of Tropical Insect Science , Volume 15 , Issue 4-5 , October 1994 , pp. 503 - 506
- Copyright
- Copyright © ICIPE 1994
References
REFERENCES
Borovsky, D. and Spielman, A. (1986) Host regulated developmental mechanisms in vector arthropods. Proc. Vero Beach Symp., pp. 125–129. IFAS Florida Medical Entomology Laboratory, Rorida, USA.Google Scholar
Budavari, S., O'Neil, M. J. and Smith, A. (Eds) (1989) Methionine. In The Merck Index. 11th ed., p. 943. Merck and Company Inc., Rahway, New Jersey.Google Scholar
Chaberek, S. and Martell, A. E. (1959) Organic Sequestering Agents, p. 548. John Wiley and Sons, New York.Google Scholar
Colman, R. F. (1968) J. Biol. Chem. 243, 2454 c.f. Liu T. (1977) The role of sulfur in proteins. In The Proteins (Edited by Neurath, H., Hill, R. L. and Boeder, C.), Vol. III, pp. 239–402. Academic Press, New York.Google Scholar
Gatel, F., Fekete, J. and Grosjean, F. (1989) A note on the use of spring pea (Pisum sativum Hortense) in diets of weaned pigs. Anim. Prod. 49, 330–332.Google Scholar
Kar, M. and Mishra, D. B. (1976) Catalase, peroxidase and polyphenoloxidase activities during rice leaf senescence. Plant Physiol. 57, 315–319.CrossRefGoogle ScholarPubMed
Kumar, K. B. and Khan, P. A. (1983) Age related changes in catalase and peroxidase activities in the excised leaves of Eleusine coracana Gaetrn. CV PR202 during senescence. Exp. Gerontol. 18, 409–417.CrossRefGoogle Scholar
Lippman, R. D. (1980) Chemiluminescent measurement of free radicals and antioxidant molecular-protection inside living rat-mitochondria. Exp. Gerontol. 15, 339–351.CrossRefGoogle ScholarPubMed
Lippman, R. D. (1981) The prolongation of life: A comparison of antioxidants and geroprotectors vs. Superoxide in human mitochondria. J. Gerontol. 36, 550–557.CrossRefGoogle Scholar
Marklund, S. L., Oreland, L., Perdahl, E. and Winblad, B. (Eds) (1983) Superoxide dismutase activity in brain from chronic alcoholics. In Drug and Alcohol Dependence. Vol. XII, pp. 209–215. Elsevier Scientific Publishers (Ireland) Limited, Ireland.Google Scholar
Massie, H. R. (1988) Chemicals. In Drosophila as a Model Organism for Ageing Studies (Edited by Lints, F. A. and Soliman, M. H.), pp. 59–70. Blackie and Son Limited, Glasgow.CrossRefGoogle Scholar
Niegdauz, B. M. and Ravin, V. K. (1984) The effect of physiologically active compounds on the life span of nematode, Caenorhabditis elegans. Zh. Biol. 44, 835–841.Google Scholar
Nohl, H., Hegner, D. and Summer, K. H. (1979) Responses of mitochondrial Superoxide dismutase, catalase and glutathione peroxidase activities to ageing. Mech. Age. Develop. 11, 145–152.CrossRefGoogle Scholar
Oshino, N., Chance, B., Sies, H. and Buchner, T. (1973) The role of hydrogen peroxide generation in perfused rat liver and the reaction of catalase compound I and hydrogen donors. Arch. Blochem. 154, 117–131.CrossRefGoogle ScholarPubMed
Placer, Z. A., Cashman, L. L. and Johnson, B. L. (1966) Estimation of product of lipid peroxidation (malondialdehyde) in biochemical systems. Anal. Biochem. 16, 359–364.CrossRefGoogle Scholar
Sohal, R. S. and Allen, R. G. (1986) Relationship between oxygen metabolism, ageing and development. Adv. Free Rad. Biol. Med. 2, 117–160.CrossRefGoogle Scholar
Sohal, R. S., Sohal, B. H. and Brunk, U. T. (1990) Relationship between antioxidant defenses and longevity in different mammalian species. Mech. Age. Develop. 53, 217–227.CrossRefGoogle ScholarPubMed
Solberg, J., Buttery, P. J. and Boorman, K. N. (1971) Br. Poul. Sci. 12, 297. c.f.CrossRefGoogle Scholar
Buttery, P. J. and Boorman, K. N. (1976) The energetic efficiency of amino acidmetabolism. In Protein Metabolism and Nutrition (Edited by Cole, D. J. A. et al.), pp. 197–206. Butterworths, London.Google Scholar
Wadhwa, R., Kaur, M. and Sharma, S. P. (1988) An antioxidant induced alteration in peroxidase activity in ageing Zaprionus paravittiger (Diptera). Mech. Age. Develop. 45, 277–283.CrossRefGoogle ScholarPubMed
Wadhwa, R. and Sharma, S. P. (1987) Studies on catalase in ageing Zaprionus paravittiger with special reference to an antioxidant feeding. Mech. Age. Develop. 40, 139–147.CrossRefGoogle Scholar