Advertisement

Planta

, Volume 140, Issue 3, pp 221–225 | Cite as

Superoxide dismutase: An enzyme system for the study of micronutrient interactions in plants

  • Luís A. del Río
  • Francisca Sevilla
  • Manuel Gómez
  • Juan Yañez
  • Julio López
Article

Abstract

The effect of different Mn levels on the isozyme pattern of superoxide dismutase was investigated. Pisum sativum L. plants were grown in nutrient solutions containing three Mn concentrations: 0.005 μg/ml (deficient), 0.05 μg/ml (low), and 0.5 μg/ml (optimum). Leaf extracts contained three electrophoretically distinct superoxide dismutases (SOD), two of which were inhibited by cyanide and were probably Cu-Zn-SODs, while the third one was CN-insensitive and could be either an Mn- or an Fe-SOD. At 0.005 μg/ml Mn supply the CN-insensitive SOD was significantly depressed at 15, 30, and 45 days of growth, whereas at 0.05 μg/ml Mn this isozyme was significantly decreased only at 45 days growth. The two CN-sensitive SODs were inversely related to the CN-resistant enzyme, the activities of the former enzymes being significantly increased at Mn-deficient levels throughout plant growth. Metal determinations of the plants showed that at low concentrations of Mn in the nutrient media, copper and zinc content of leaves increased: the lower the Mn level, the higher the increase produced. The CN-resistant SOD activity, as judged by its dependency on Mn, appears to be an Mn-SOD rather than an Fe-SOD. In the light of the results obtained, the use of the enzyme system superoxide dismutase for the study of the role and interactions between Mn, Cu, and Zn in the plant cell is proposed.

Key words

Manganese Micronutrient interactions Pisum Superoxide dismutase 

Abbreviations

EDTA

ethylenediaminotetraacetic acid

NBT

nitro blue terazolium

SOD

superoxide dismutase (EC 1.15.1.1)

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Arron, G.P., Henry, L., Palmer, J.M., Hall, D.O.: Superoxide dismutases in mitochondria from Helianthus tuberosus and Neurospora crassa. Biochem. Soc. Trans. 4, 618–620 (1976)Google Scholar
  2. Asada, K., Urano, M., Takahashi, M.: Subcellular location of superoxide dismutase in spinach leaves and preparation and properties of crystalline spinach superoxide dismutase. Eur. J. Biochem. 36, 257–266 (1973)Google Scholar
  3. Asada, K., Kanematsu, S., Takahashi, M., Kono, Y.: Superoxide dismutases in photosynthetic organisms. In: Iron and copper proteins, pp. 551–564, Yasunobu, K.T., Mower, H.F., Hayaishi, O., eds., New York: Plenum 1976Google Scholar
  4. Asada, K., Kanematsu, S., Uchida, K.: Superoxide dismutases in photosynthetic organisms. Absence of the cuprozinc enzyme in eukaryotic algae. Arch. Biochem. Biophys. 179, 243–256 (1977)Google Scholar
  5. Bar-Akiva, A.: Functional aspects of mineral nutrients in use for the evaluation of plant nutrient requirement. In: Recent advances in plant nutrition, vol. 1, pp. 115–139, Samish, R.M., ed. New York-London-Paris: Gordon and Breach 1971Google Scholar
  6. Beauchamp, C.O., Fridovich, I.: Superoxide dismutase. Improved assays and an assay applicable to acrylamide gels. Anal. Biochem. 44, 276–287 (1971)Google Scholar
  7. Beauchamp, C.O., Fridovich, I.: Isozymes of superoxide dismutase from wheat germ. Biochim. Biophys. Acta 317, 50–64 (1973)Google Scholar
  8. C.I.I.A.F.: Méthodes de référence pour la détermination des élément minéraux dans les végétaux. Détermínation des éléments Ca, Mg, Fe, Mn, Zn et Cu par absorption atomique. Oléagineux 28, 87–92 (1973)Google Scholar
  9. Davis, B.J.: Disc gel electrophoresis. Ann. N. Y. Acad. Sci. 121, 404–427 (1964)Google Scholar
  10. Del Río, L.A., Gómez, M., Yañez, J., Leal, A., López, J.: Iron deficiency in pea plants. Effect on catalase, peroxidase, chlorophyll and proteins of leaves. Plant and Soil 54, in press (1977)Google Scholar
  11. Fridovich, I.: Superoxide dismutases. Adv. Enzymol. 41, 35–97 (1974)Google Scholar
  12. Giannopolitis, C.N., Ries, S.K.: Superoxide dismutases. I. Occurrence in higher plants. Plant Physiol. 59, 309–314 (1977)Google Scholar
  13. Lumsden, J., Hall, D.O.: Soluble and membrane-bound superoxide dismutases in a blue-green alga (Spirulina) and spinach. Biochem. Biophys. Res. Commun. 58, 35–41 (1974)Google Scholar
  14. McCord, J.M., Fridovich, I.: Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J. Biol. Chem. 244, 6049–6055 (1969)Google Scholar
  15. Potty, V.H.: Determination of proteins in the presence of phenols and pectins. Anal. Biochem. 29, 535–539 (1969)Google Scholar
  16. Sacher, J.A.: Senescence and postharvest physiology. Ann. Rev. Plant Physiol. 24, 197–224 (1973)Google Scholar
  17. Sawada, Y., Ohyama, T., Yamazaki, I.: Preparation and physicochemical properties of green pea superoxide dismutase. Biochim. Biophys. Acta 268, 305–312 (1972)Google Scholar
  18. Vallee, B.L., Wacker, W.E.C.: Metalloproteins. In: The proteins. Composition, structure and function, vol. V, 2nd edition, pp. 25–60, Neurath, H., ed., New York-London: Academic Press 1970Google Scholar
  19. Weisiger, R.A., Fridovich, I.: Superoxide dismutase. Organelle specificity. J. Biol. Chem. 248, 3582–3592 (1973)Google Scholar

Copyright information

© Springer-Verlag 1978

Authors and Affiliations

  • Luís A. del Río
    • 1
  • Francisca Sevilla
    • 1
  • Manuel Gómez
    • 1
  • Juan Yañez
    • 1
  • Julio López
    • 1
  1. 1.Sección de Bioquímica, Estación Experimental del ZaidínC.S.I.C.GranadaSpain

Personalised recommendations