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Plant Physiology 95:21-28 (1991)
© 1991 American Society of Plant Biologists

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Metabolism and Enzymology

Isolation, Purification, and Subcellular Localization of Isozymes of Superoxide Dismutase from Scots Pine (Pinus sylvestris L.) Needles 1

Gunnar Wingsle, Per Gardeström, Jan-Erik Hällgren and Stanislaw Karpinski

Department of Forest Genetics and Plant Physiology, Swedish University of Agricultural Sciences, S-901 83 Umeå, Sweden, Department of Plant Physiology, University of Umeå, S-90187 Umeå, Sweden

Two of four isozymes of superoxide dismutase (SOD) (EC 1.15.1.1) were purified from Scots pine (Pinus sylvestris L.) needles. One form was cytosolic (SOD-1) and the other was associated with chloroplasts (SOD-3). The holoenzyme molecular masses was estimated at approximately 35 kilodaltons by gel filtration. The subunit molecular weight of the dimeric enzymes was estimated to 16.5 kilodaltons (SOD-1) and 20.4 kilodaltons (SOD-3) on sodium dodecyl sulfatepolyacrylamide gels. The NH2-terminal sequence of the pine enzymes showed similarities to other purified superoxide dismutases located in the corresponding compartment. The cytosolic form revealed two additional amino acids at position 1 and 2 at the NH2-terminal. Both forms were cyanide- and hydrogenperoxide-sensitive and SOD-3 was found to contain approximately one copper atom per subunit, indicating that they belong to the cupro-zinc SODs. The isoelectric point was 4.9 and 4.5 for SOD-1 and SOD-3, respectively.

1 This work was financially supported by the Swedish Council for Forestry and Agricultural Research.




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I. J. Odrzykoski
Inheritance and Subcellular Localization of Triose-Phosphate Isomerase in Dwarf Mountain Pine (Pinus mugo)
J. Hered., May 1, 2001; 92(3): 271 - 274.
[Abstract] [Full Text] [PDF]


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Copyright © 1991 by the American Society of Plant Biologists