Abstract
The 24 h effect of low (20°C) and high (43°C) temperature on the antioxidant enzyme activities and lipid peroxidation was investigated in intact cells of the cyanobacteriumSynechocystis PCC 6803 grown at 36°C. At low temperature treated cells, the superoxide dismutase, catalase and glutathione peroxidase activities were significantly higher and the protein content lower than in high temperature treated cells. The increase of hydroxyl free radical level and malonyldialdehyde formation, when algal cells were exposed to low temperature, were due to the stimulated production of superoxide radicals O2 − and hydrogen peroxide (H2O2).
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
Abelovich, A., Kellenberg, D., Shilo, M.: Effect of photooxidative conditions on levels of superoxide dismutase inAnacystis nidulans.—Photochem. Photobiol.19: 379–382, 1974.
Allen, C.F., Good, B., Davis, H.F., Fowler, S.D.: Plant and chloroplast lipids I. Separation and composition of major spinach lipids.—Biochem. biophys. Res. Commun.15: 424–430, 1964.
Allen, M.M.: Simple conditions for growth of blue-green algae on plates.—J. Phycol.4: 1–4, 1968.
Beauchmamp, C., Fridovich, I.: Superoxide dismutase: Improved assay and an assay application to acrylamide gels.—Anal. Biochem.44: 276–287, 1971.
Beers, R.F. Jr., Sizer, I.W.: Spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase.—J. biol. Chem.195: 133–140, 1952.
Brand, J.J.: Spectral changes inAnacystis nidulans induced by chilling.—Plant Physiol.59: 970–973, 1977.
Chiu, D.T., Stults, F.H., Tappal, A.L.: Purification and properties of rat lung soluble glutathione peroxidase.—Biochim. biophys. Acta445: 558–566, 1976.
Deng, I.C.: Effect of ice storage on free fatty acid production and lipid oxidation in mullet muscle.—J. Food Sci.43: 337–340, 1978.
Dykens, G.A., Malcolm-Shick, G.: Oxygen production by endosymbiotic algae controls superoxide dismutase activity in their animal host.—Nature297: 579–580, 1982.
Fridovich, I.: Superoxide dismutase.—In: Hayaishi, O. (ed.): Molecular Mechanism of Oxygen Activation, Pp. 453–477. Academic Press, New York-London 1974.
Fridovich, I.: Biology of oxygen radicals.—Science201: 875–880, 1978.
Jansz, E.R., Maclean, E.I.: The effect of cold shock on the blue green algaAnacystis nidulans.—Can. J. Microbiol.19: 381–387, 1973.
Lowry, O.H., Rosebrough, N.J., Farr, A.L., Randall, R.J.: Protein measurement with the Folin phenol reagent.—J. biol. Chem.193: 265–275, 1951.
Matkovics, B., Novak, R., Hoang Duc, H., Szabo, L., Varga, Sz.I., Zalesna, G.A.: Comparative study on some more important experimental peroxide metabolism enzymes.—Comp. Biochem. Physiol.56B: 31–34, 1977.
Matkovics, B., Szabo, L., Varga, I.: [Determination of lipid peroxidation, reduced glutathione and metabolic enzyme activities in the biological samples].—Laboratorium Diagnosztika15: 248–250, 1988. [In Hung.]
Matkovics, B., Szöllösine, V.I., Nová, Z.: [Determination of oxygen amounts in the biological samples].—Laboratorium Diagnosztika18: 40–46, 1991. [In Hung.]
McCord, J.M., Keele, Jr. B.B., Fridovich, I.: An enzyme based theory of obligate anaerobiosis: The physiological function of superoxide dismutase.—Proc. nat. Acad. Sci. USA68: 1024–1027, 1971.
Misra, H.P., Fridovich, I.: The role of superoxide anion in the antioxidant of epinephrine and a simple assay for superoxide dismutase.—J. biol. Chem.247: 3170–3175, 1972.
Patterson, C.O.P., Myers, J.: Photosynthetic production of hydrogen peroxide byAnacystis nidulans. —Plant Physiol.51: 104–109, 1973.
Placer, Z.A., Custhman, L., Johnson, B.C.: Estimation of product of lipid peroxidation (malonyldialdehyde) in biochemical system.—Biochemistry16: 359–364, 1966.
Rao, V., Brand, J.J., Myers, T.: Cold shock syndrome inAnacystis nidulans.—Plant Physiol.59: 965–969, 1977.
Sedlak, I., Lindsey, F.H.: Estimation of total proteinbound and non protein sulphydryl group in tissue with Ellmanis reagent.—Anal. Biochem.25: 192–205, 1958.
Stanier, R.Y., Cohen-Bazire, G.: Phototropic procaryotes, the cyanobacterium.—Annu. Rev. Microbiol.31: 225–274, 1977.
Vigh, L., Lehel, C.S., Török, Zs., Gombos, Z., Balogh, N., Horváth, I.: Factors affecting thylakoid thermal stability in cyanobacteriumSynechocystis sp. PCC 6803.—In: Quinn, P.J., Harwood, J.L. (ed.): Plant Lipid Biochemistry: Structure and Utilization. Pp. 373–381. Portland Press, London 1990.
Winterbourn, C.C.: Factor that influencing the deoxyribose oxidation assay for Fentom reaction products.—Free Radical Biol. Med.11: 353–360, 1991.
Witas, H., Gabryelak, T., Matkovics, B.: Comparative studies on superoxide dismutase and catalase activities in livers of fish and other vertbrates.—Comp. Biochem. Physiol.69: 345–349, 1984.
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
El-Sheekh, M.M., Rady, A.A. Temperature shift-induced changes in the antioxidant enzyme system of cyanobacteriumSynechocystis PCC 6803. Biol Plant 37, 21–25 (1995). https://doi.org/10.1007/BF02912994
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1007/BF02912994