Skip to main content
Log in

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

  • Published:
Planta Aims and scope Submit manuscript

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.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

Abbreviations

EDTA:

ethylenediaminotetraacetic acid

NBT:

nitro blue terazolium

SOD:

superoxide dismutase (EC 1.15.1.1)

References

  • 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 

  • 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 

  • 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 1976

    Google Scholar 

  • 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 

  • 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 1971

    Google Scholar 

  • Beauchamp, C.O., Fridovich, I.: Superoxide dismutase. Improved assays and an assay applicable to acrylamide gels. Anal. Biochem. 44, 276–287 (1971)

    Google Scholar 

  • Beauchamp, C.O., Fridovich, I.: Isozymes of superoxide dismutase from wheat germ. Biochim. Biophys. Acta 317, 50–64 (1973)

    Google Scholar 

  • 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 

  • Davis, B.J.: Disc gel electrophoresis. Ann. N. Y. Acad. Sci. 121, 404–427 (1964)

    Google Scholar 

  • 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)

  • Fridovich, I.: Superoxide dismutases. Adv. Enzymol. 41, 35–97 (1974)

    Google Scholar 

  • Giannopolitis, C.N., Ries, S.K.: Superoxide dismutases. I. Occurrence in higher plants. Plant Physiol. 59, 309–314 (1977)

    Google Scholar 

  • 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 

  • McCord, J.M., Fridovich, I.: Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J. Biol. Chem. 244, 6049–6055 (1969)

    Google Scholar 

  • Potty, V.H.: Determination of proteins in the presence of phenols and pectins. Anal. Biochem. 29, 535–539 (1969)

    Google Scholar 

  • Sacher, J.A.: Senescence and postharvest physiology. Ann. Rev. Plant Physiol. 24, 197–224 (1973)

    Google Scholar 

  • Sawada, Y., Ohyama, T., Yamazaki, I.: Preparation and physicochemical properties of green pea superoxide dismutase. Biochim. Biophys. Acta 268, 305–312 (1972)

    Google Scholar 

  • 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 1970

    Google Scholar 

  • Weisiger, R.A., Fridovich, I.: Superoxide dismutase. Organelle specificity. J. Biol. Chem. 248, 3582–3592 (1973)

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

del Río, L.A., Sevilla, F., Gómez, M. et al. Superoxide dismutase: An enzyme system for the study of micronutrient interactions in plants. Planta 140, 221–225 (1978). https://doi.org/10.1007/BF00390251

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00390251

Key words

Navigation