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Alterations in Soluble Class III Peroxidases of Maize Shoots by Flooding Stress
- Source :
- Proteomes, Proteomes; Volume 2; Issue 3; Pages: 303-322, Proteomes, Vol 2, Iss 3, Pp 303-322 (2014)
- Publication Year :
- 2014
- Publisher :
- MDPI, 2014.
-
Abstract
- Due to changing climate, flooding (waterlogged soils and submergence) becomes a major problem in agriculture and crop production. In the present study, the effect of waterlogging was investigated on peroxidases of maize (Zea mays L.) leaves. The plants showed typical adaptations to flooding stress, i.e., alterations in chlorophyll a/b ratios and increased basal shoot diameter. Seven peroxidase bands could be detected by first dimension modified SDS-PAGE and 10 bands by first dimension high resolution Clear Native Electrophoresis that altered in dependence on plant development and time of waterlogging. Native isoelectric focusing revealed three acidic to neutral and four alkaline guaiacol peroxidases that could be further separated by high resolution Clear Native Electrophorese in the second dimension. One neutral peroxidase (pI 7.0) appeared to be down-regulated within four hours after flooding, whereas alkaline peroxidases (pI 9.2, 8.0 and 7.8) were up-regulated after 28 or 52 h. Second dimensions revealed molecular masses of 133 kDa and 85 kDa for peroxidases at pI 8.0 and 7.8, respectively. Size exclusion chromatography revealed native molecular masses of 30–58 kDa for peroxidases identified as class III peroxidases and ascorbate peroxidases by mass spectrometry. Possible functions of these peroxidases in flooding stress will be discussed.
- Subjects :
- native PAGE
guaiacol peroxidases
shoot
Clinical Biochemistry
Size-exclusion chromatography
lcsh:QR1-502
Biochemistry
lcsh:Microbiology
Article
Basal shoot
chemistry.chemical_compound
flooding
Structural Biology
Zea mays L
Botany
Molecular Biology
soluble proteins
biology
Chemistry
Isoelectric focusing
food and beverages
Shoot
biology.protein
Guaiacol
water logging
Ascorbate Peroxidases
Waterlogging (agriculture)
Peroxidase
Subjects
Details
- Language :
- English
- ISSN :
- 22277382
- Volume :
- 2
- Issue :
- 3
- Database :
- OpenAIRE
- Journal :
- Proteomes
- Accession number :
- edsair.doi.dedup.....d37578f2ac587521f9c8818dfb1ba2d0