ISOLATION, PURIFICATION, AND SUBCELLULAR-LOCALIZATION OF ISOZYMES OF SUPEROXIDE-DISMUTASE FROM SCOTS PINE (PINUS-SYLVESTRIS L) NEEDLES
1991 (English)In: Plant Physiology, ISSN 0032-0889, E-ISSN 1532-2548, Vol. 95, no 1, 21-28 p.Article in journal (Refereed) Published
Two of four isozymes of superoxide dismutase (SOD) (EC 184.108.40.206) 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.
Place, publisher, year, edition, pages
1991. Vol. 95, no 1, 21-28 p.
IdentifiersURN: urn:nbn:se:umu:diva-46916DOI: 10.1104/pp.95.1.21ISI: A1991ET77200004OAI: oai:DiVA.org:umu-46916DiVA: diva2:447234