TY  - JOUR
AU  - Momčilović, Ivana
AU  - Pantelic, Danijel
AU  - Hfidan, Masoud
AU  - Savic, Jelena
AU  - Vinterhalter, Dragan
PY  - 2014
UR  - https://radar.ibiss.bg.ac.rs/handle/123456789/2180
AB  - Superoxide dismutase (SOD) in-gel activity assay with selective
   inhibitors (KCN and H2O2) is one of the most commonly used methods for
   identification of SOD isoform types, i.e., FeSOD, MnSOD or Cu/ZnSOD, and
   evaluation of oxidative stress response in plants. However, there are
   potential pitfalls that surround this assay, such as problem to detect
   isoforms with low activity, comigration of SOD isoforms or application
   of inappropriate inhibitor concentration. We propose an improved method
   based on the combination of in-gel analysis of SOD activity and
   native-PAGE immunoblotting for identification of isoforms and
   determination of SOD isoenzyme activity pattern in potato. Depending on
   cultivar and growing conditions, one MnSOD, 3 FeSOD and 5-6 Cu/ZnSOD
   isoforms were identified in potato leaves. The most important
   qualitative difference between ex vitro- and in vitro-grown plants was
   the presence of additional FeSOD and Cu/ZnSOD isoforms in plantlets
   grown in vitro. Compared with results of in-gel activity assay with
   selective inhibitors, new method allowed accurate identification of
   comigrating FeSOD and Cu/ZnSOD isoforms and two protein bands of
   ambiguous identities. Potato SODs were also characterized by SDS-PAGE
   immunoblotting and single MnSOD (23.6 kDa), three Cu/ZnSOD polypeptides
   (17.9, 17 and 16.3 kDa) and single FeSOD (25.1 kDa) polypeptide were
   detected in leaves of four examined cultivars. The difference in the
   number of FeSOD and Cu/ZnSOD isoforms/polypeptides between native-PAGE
   and SDS-PAGE immunoblots suggests that SOD proteins may have undergone
   post-translational modifications affecting protein mobility or existence
   of isoforms that differ from each other in total protein charge, but not
   in molecular weight.
T2  - Acta Physiologiae Plantarum
T1  - Improved procedure for detection of superoxide dismutase isoforms in
 potato, Solanum tuberosum L.
IS  - 8
VL  - 36
DO  - 10.1007/s11738-014-1583-z
SP  - 2059
EP  - 2066
ER  - 

@article{
author = "Momčilović, Ivana and Pantelic, Danijel and Hfidan, Masoud and Savic, Jelena and Vinterhalter, Dragan",
year = "2014",
abstract = "Superoxide dismutase (SOD) in-gel activity assay with selective
   inhibitors (KCN and H2O2) is one of the most commonly used methods for
   identification of SOD isoform types, i.e., FeSOD, MnSOD or Cu/ZnSOD, and
   evaluation of oxidative stress response in plants. However, there are
   potential pitfalls that surround this assay, such as problem to detect
   isoforms with low activity, comigration of SOD isoforms or application
   of inappropriate inhibitor concentration. We propose an improved method
   based on the combination of in-gel analysis of SOD activity and
   native-PAGE immunoblotting for identification of isoforms and
   determination of SOD isoenzyme activity pattern in potato. Depending on
   cultivar and growing conditions, one MnSOD, 3 FeSOD and 5-6 Cu/ZnSOD
   isoforms were identified in potato leaves. The most important
   qualitative difference between ex vitro- and in vitro-grown plants was
   the presence of additional FeSOD and Cu/ZnSOD isoforms in plantlets
   grown in vitro. Compared with results of in-gel activity assay with
   selective inhibitors, new method allowed accurate identification of
   comigrating FeSOD and Cu/ZnSOD isoforms and two protein bands of
   ambiguous identities. Potato SODs were also characterized by SDS-PAGE
   immunoblotting and single MnSOD (23.6 kDa), three Cu/ZnSOD polypeptides
   (17.9, 17 and 16.3 kDa) and single FeSOD (25.1 kDa) polypeptide were
   detected in leaves of four examined cultivars. The difference in the
   number of FeSOD and Cu/ZnSOD isoforms/polypeptides between native-PAGE
   and SDS-PAGE immunoblots suggests that SOD proteins may have undergone
   post-translational modifications affecting protein mobility or existence
   of isoforms that differ from each other in total protein charge, but not
   in molecular weight.",
journal = "Acta Physiologiae Plantarum",
title = "Improved procedure for detection of superoxide dismutase isoforms in
 potato, Solanum tuberosum L.",
number = "8",
volume = "36",
doi = "10.1007/s11738-014-1583-z",
pages = "2059-2066"
}

Momčilović, I., Pantelic, D., Hfidan, M., Savic, J.,& Vinterhalter, D.. (2014). Improved procedure for detection of superoxide dismutase isoforms in
 potato, Solanum tuberosum L.. in Acta Physiologiae Plantarum, 36(8), 2059-2066.
https://doi.org/10.1007/s11738-014-1583-z

Momčilović I, Pantelic D, Hfidan M, Savic J, Vinterhalter D. Improved procedure for detection of superoxide dismutase isoforms in
 potato, Solanum tuberosum L.. in Acta Physiologiae Plantarum. 2014;36(8):2059-2066.
doi:10.1007/s11738-014-1583-z .

Momčilović, Ivana, Pantelic, Danijel, Hfidan, Masoud, Savic, Jelena, Vinterhalter, Dragan, "Improved procedure for detection of superoxide dismutase isoforms in
 potato, Solanum tuberosum L." in Acta Physiologiae Plantarum, 36, no. 8 (2014):2059-2066,
https://doi.org/10.1007/s11738-014-1583-z . .