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ISOLATION, PURIFICATION, AND SUBCELLULAR-LOCALIZATION OF ISOZYMES OF SUPEROXIDE-DISMUTASE FROM SCOTS PINE (PINUS-SYLVESTRIS L) NEEDLES
Umeå University, Faculty of Science and Technology, Umeå Plant Science Centre (UPSC).
Umeå University, Faculty of Science and Technology, Department of Plant Physiology. Umeå University, Faculty of Science and Technology, Umeå Plant Science Centre (UPSC).ORCID iD: 0000-0001-5900-7395
1991 (English)In: Plant Physiology, ISSN 0032-0889, E-ISSN 1532-2548, Vol. 95, no 1, 21-28 p.Article in journal (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
1991. Vol. 95, no 1, 21-28 p.
Identifiers
URN: urn:nbn:se:umu:diva-46916DOI: 10.1104/pp.95.1.21ISI: A1991ET77200004OAI: oai:DiVA.org:umu-46916DiVA: diva2:447234
Available from: 2011-10-11 Created: 2011-09-16 Last updated: 2017-12-08

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