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Purification and Properties of Manganese Superoxide Dismutase from Norway Spruce (Picea abies L. Karst) |
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| Authors: | Kroniger Werner; Rennenberg Heinz; Tadros Monier H; Polle Andrea |
| Institution: | 1 Fraunhofer Institut für Atmosphärische Umweltforschung Kreuzeckbahnstr 19, D-82467 Garmisch-Partenkirchen, F.R.G. 2 Albert-Ludwigs-Universität, Institut für Forstbotanik und Baumphysiologie, Professur für Baumphysiologie Am Flughafen 17, D-79085 Freiburg, F.R.G. 3 Albert-Ludwigs-Universität, Institut für Biologie 2, Mikrobiologie Schänzlestr. 1, D-79085 Freiburg, F.R.G. |
| Abstract: | A manganese-containing superoxide dismutase (SOD; EC 1.15.1.1 EC] )was purified to electrophoretic homogeneity from seeds of Norwayspruce (Picea abies L.). The apparent molecular mass of thepurified enzyme was 86 kDa, as determined by gel filtration.The subunit molecular mass, estimated by SDS-polyacrylamidegel electrophoresis, was 22 kDa both in the presence and inthe absence of 2-mercaptoethanol. Thus, the native enzyme isa homotetramer with subunits that were not linked by disulfidebonds. The isoelectric point of this Mn-SOD was 5.5. The specificactivity of the Mn-SOD was strongly pH-dependent and was 400units per nmol SOD at pH 7.8 and 30 units per nmol SOD at pH10.4. The first 25 amino acid residues in the amino terminalregion of spruce Mn-SOD exhibited a high degree of sequencehomology to those of Mn-SODs from other organisms. In Mn-deficientneedles the activity of Mn-SOD was only half of that in non-deficientneedles, whereas the activity of CuZn-SOD was doubled. (Received May 20, 1994; Accepted October 31, 1994) |
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