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  • 1
    Online Resource
    Online Resource
    Berlin, Heidelberg :Springer Berlin / Heidelberg,
    Keywords: Plant cellular signal transduction. ; Active oxygen. ; Electronic books.
    Description / Table of Contents: The production of reactive oxygen species in plants used to be thought harmful, but recent research shows ROS to be key regulators of plant metabolism, morphology and development. This book offers the latest in the field, highlighting new data and concepts.
    Type of Medium: Online Resource
    Pages: 1 online resource (244 pages)
    Edition: 1st ed.
    ISBN: 9783642003905
    Series Statement: Signaling and Communication in Plants Series
    DDC: 571.742
    Language: English
    Note: Rio_FM.pdf -- Rio_Ch01.pdf -- Rio_Ch02.pdf -- Rio_Ch03.pdf -- Rio_Ch04.pdf -- Rio_Ch05.pdf -- Rio_Ch06.pdf -- Rio_Ch07.pdf -- Rio_Ch08.pdf -- Rio_Ch09.pdf -- Rio_Ch10.pdf -- Rio_Ch11.pdf -- Rio_Ch12.pdf -- Rio_Ch13.pdf -- Rio_Ch14.pdf -- Rio_Index.pdf.
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  • 2
    Online Resource
    Online Resource
    Singapore :Springer Singapore Pte. Limited,
    Keywords: Peroxisomes. ; Electronic books.
    Type of Medium: Online Resource
    Pages: 1 online resource (488 pages)
    Edition: 1st ed.
    ISBN: 9789811322334
    Series Statement: Subcellular Biochemistry Series ; v.89
    Language: English
    Note: Intro -- Preface -- References -- Contents -- Mass Spectrometry-Based Organelle Proteomics -- 1 Proteome of Plant Peroxisomes -- Abstract -- 1 Introduction -- 2 MS-Based Peroxisome Proteome Studies in Plants -- 3 An Update on Arabidopsis Peroxisome Proteins and Their Functions -- 3.1 Biogenesis and Dynamics of Peroxisomes -- 3.2 Fatty Acid Catabolism and Hormone Biosynthesis -- 3.3 Photorespiration -- 3.4 The Glyoxylate Cycle -- 3.5 Detoxification of ROS and Methylglyoxal -- 3.6 Biosynthesis of Phylloquinone, Biotin and CoA -- 3.7 The Mevalonic Acid (MVA) Pathway -- 3.8 Catabolism of Polyamines, Urate, Pseudouridine and Sulfite -- 3.9 Amino Acid Metabolism -- 3.10 Pathogen Response -- 3.11 Metabolism of NADPH and NADH -- 3.12 Peroxisomal Transporters for Metabolites and Cofactors -- 3.13 Nucleotide Homeostasis -- 3.14 Phosphoregulation -- 3.15 Molecular Chaperones and Proteases -- 3.16 Other Peroxisomal Proteins -- 4 Conclusions and Perspectives -- Acknowledgements -- References -- 2 Defining the Mammalian Peroxisomal Proteome -- Abstract -- 1 Introduction -- 2 Mass Spectrometry-Based Studies of Mammalian Peroxisomes -- 3 Definition of the Mammalian Peroxisomal Proteome -- 3.1 Proteins That Are Detected in High Frequency in Peroxisomal Fractions -- 3.2 Proteins That Are Detected in Low Frequency in Peroxisomal Fractions -- 4 Conclusions -- Acknowledgements -- References -- 3 Fungal Peroxisomes Proteomics -- Abstract -- 1 Introduction -- 2 Organellar Proteomics on Peroxisomes in Fungi -- 2.1 Organellar Proteomics on Peroxisomes from S. Cerevisiae -- 2.2 The Proteome of Peroxisomes in N. Crassa -- 2.3 Identification of Peroxisomal Matrix Proteins in P. Chrysogenum -- 3 Perspectives -- Acknowledgements -- References -- 4 The Craft of Peroxisome Purification-A Technical Survey Through the Decades -- Abstract -- 1 Introduction. , 2 Isolation of PO from Liver and Kidney -- 2.1 Liver Peroxisomes -- 2.2 Kidney Peroxisomes -- 3 Peroxisome Isolation from Brain Tissue-A Still Unsolved Problem -- 4 Peroxisome Isolation from Yeast and Other Fungi -- 5 Peroxisome/Glyoxysome Purification from Plants -- 6 The Limits of Density Gradient Centrifugation-The Development of Alternative Purification Techniques -- 7 The Era of Proteomics-Opposing Approaches to Characterize Organelle Proteomes -- 8 Challenges for the Future -- Acknowledgements -- References -- Predicting Peroxisomal Proteomes -- 5 Prediction of Peroxisomal Matrix Proteins in Plants -- Abstract -- 1 Prediction of PTS1 Proteins -- 1.1 Canonical Versus Non-canonical PTS1s -- 1.2 Prediction Algorithms for PTS1 Proteins -- 1.3 Prediction and Analysis of Peroxisome Targeting Efficiency -- 2 PTS2 Nonapeptide Definition and Prediction of PTS2 Proteins -- 3 Conclusions and Future Perspectives -- References -- 6 The Obvious and the Hidden: Prediction and Function of Fungal Peroxisomal Matrix Proteins -- Abstract -- 1 Peroxisomes in Fungi -- 2 Predicting Peroxisomal Proteins -- 3 Cryptic Peroxisomal Proteins -- 3.1 Weak Peroxisomal Targeting Signals Promote Dual Targeting -- 3.2 Differential Splicing and More: Alternative Transcripts Encoding Peroxisomal Isoforms -- 3.3 Translational Stop Codon Readthrough: A Widely Conserved Mechanism to Create Peroxisomal Isoforms -- 3.4 Peroxisomal Matrix Proteins Without PTS: The Really Hidden Ones -- 4 Dual Targeting Reveals a Broader Metabolic Capacity of Fungal Peroxisomes -- References -- 7 Predicting Peroxisomal Targeting Signals to Elucidate the Peroxisomal Proteome of Mammals -- Abstract -- 1 Introduction -- 2 Elucidation of the Peroxisomal Proteome -- 3 Predicting the Peroxisomal Proteome -- 3.1 Concept -- 3.2 Peroxisomal Protein Transport -- 3.3 Peroxisomal Targeting Signals. , 3.3.1 Targeting Signals for Matrix Proteins -- 3.3.2 Targeting Signals for Membrane Proteins -- 3.4 Computational Algorithms to Predict the Subcellular Localization of Proteins -- 3.4.1 Prediction Algorithms to Identify Targeting Signals -- Prediction Algorithms Based on the Conservation Pattern at Individual Positions of the Targeting Signal -- Generating Prediction Algorithms for Targeting Signals by Combining Various Properties and Considering the Context -- 3.4.2 Prediction Algorithms to Classify Proteins into Groups Sharing the Same Subcellular Compartment -- 3.5 Available Prediction Algorithms for the Identification of Peroxisomal Proteins -- 3.5.1 Prediction Algorithms for Targeting Signals -- 3.5.2 Prediction Algorithms Based on Classifiers Using General Properties of Peroxisomal Proteins -- 4 Strengths and Weaknesses of Prediction Algorithms -- 4.1 General Considerations -- 4.2 Incorrect Predictions Based on the Limitations of the Algorithm -- 4.3 Biological Background of the Misevaluation -- 4.4 Evaluation of the Quality of Prediction Algorithms -- 5 Prediction of the Peroxisomal Proteome -- 6 Summary and Outlook -- Acknowledgements -- References -- 8 Multiple Localization by Functional Translational Readthrough -- Abstract -- 1 Dual and Multiple Targeting of Proteins -- 2 Dual and Multiple Targeting to the Peroxisome and Other Organelles -- 3 Identifying the PTS1ome by Bioinformatics -- 4 The Hierarchy of Targeting Signals -- 5 Translational Readthrough -- 6 Functional Translational Readthrough Diversifies Protein Function -- 7 Functional Translational Readthrough Diversifies Protein Targeting -- 8 Omics Approaches for the Identification of Readthrough Proteins -- 9 Readthrough-Omics in Silico -- 10 Translational Readthrough as a Modification of the Genetic Code -- 11 The Physiology of Peroxisomal Malate and Lactate Dehydrogenases. , Acknowledgements -- References -- 9 Evolution of the Peroxisomal Proteome -- Abstract -- 1 Introduction -- 2 Functional Diversity of Extant Peroxisomes -- 3 Diverse but All the Same -- 4 Evolutionary Origin of Peroxisomes -- 5 Current Hypotheses on the Origin of the Peroxisome -- 6 Shaping the Peroxisomal Proteome Through Subcellular Retargeting -- 7 Secondary Loss of Peroxisomes -- 8 Concluding Remarks -- Acknowledgements -- References -- 10 Peroxisome Protein Prediction in Drosophila melanogaster -- Abstract -- 1 Introduction: Drosophila Has Been Used in the Laboratory for over 100 Years -- 2 Early Studies of Drosophila Peroxisomal Proteins -- 2.1 Analysis of Potential Peroxisome Enzymes in Drosophila Organs -- 2.2 Release of the Drosophila Genome Sequence and Peroxisome Protein Predictions -- 3 Systematic Analysis of the Drosophila Peroxisome Proteome -- 3.1 Identification of Drosophila Peroxisome Biogenesis Protein Homologs -- 3.2 Functional Characterization of Predicted Drosophila Pex Proteins -- 3.3 Drosophila Does not Seem to Employ PTS2 Mediated Protein Trafficking -- 3.4 Conservation of Drosophila Peroxisome Membrane Protein (PMP) Trafficking -- 3.5 Drosophila Peroxisome Matrix Proteins -- 4 The Effects of Overexpressing Drosophila Peroxisome Proteins -- 5 Screening for Peroxisome-Associated Proteins  in Drosophila -- 5.1 Large Scale Screens for Novel Protein Interactions -- 5.2 Proteins Regulating Peroxisome Dynamics in Drosophila S2 Cells -- 6 Developing Drosophila as a Model for Human Peroxisome Biogenesis Disorders -- 6.1 Phenotypes Associated with Defective Peroxisome Biogenesis in Drosophila -- 6.2 Analysis of the Drosophila Whole-Animal Response to Pex1 Deficiency -- 6.3 Modelling Single Peroxisome Enzyme Deficiencies Using Drosophila -- 7 Identification of Novel Peroxisome Functions Using Drosophila -- 8 Summary -- References. , Analysis of Peroxisome Proteome Interaction Networks -- 11 Using Pull Down Strategies to Analyze the Interactome of Peroxisomal Membrane Proteins in Human Cells -- Abstract -- 1 Membrane Protein Complexes in Human Peroxisomes -- 1.1 Biogenesis I-de Novo Formation, Proliferation and Division -- 1.2 Biogenesis II-Membrane and Matrix Protein Import -- 1.3 PMPs with Other Functions -- 1.3.1 Metabolite Transport -- 1.3.2 Inter-Organelle Contact Sites -- 1.3.3 Novel Functions of PMPs -- 2 Proteomic Strategies Applied to the Characterization of PMPs from Human Cells -- 2.1 MS-Based Methods for the Characterization of Human PMP Complexes -- 2.1.1 Affinity Purification Combined with High-Resolution Mass Spectrometry (AP-MS) -- 2.1.2 Proximity-Dependent Biotin Identification (BioID) -- 2.2 Critical Aspects to Consider for Experimental Design -- 3 Towards a PMP Interactome -- 3.1 The PEX14 Complex Analysis Revisited -- 3.2 PEX16 Interactome Defined by BioID -- 3.3 Comparing the Peroxin Network of Yeast and Man -- 4 Outlook -- Acknowledgements -- References -- 12 Identification of Peroxisomal Protein Complexes with PTS Receptors, Pex5 and Pex7, in Mammalian Cells -- Abstract -- 1 Introduction -- 2 Approaches to Identifying Peroxisomal Protein Import Complexes in Mammalian Cells -- 3 Identification of Peroxisomal Protein Complexes by Immunoprecipitation -- 3.1 Complexes with PTS1 Receptor Pex5 -- 3.2 Complexes with PTS2 Receptor Pex7 -- 3.3 Substrates of Intraperoxisomal Processing Enzyme, Tysnd1 -- 4 Biochemical Purification of Awp1 -- 5 Concluding Remarks -- Acknowledgements -- References -- 13 Unraveling of the Structure and Function of Peroxisomal Protein Import Machineries -- Abstract -- 1 Peroxisomal Protein Import -- 2 Peroxisomal Matrix Protein Import -- 2.1 Cargo Recognition -- 2.1.1 Pre-import Complexes -- 2.2 Docking at the Peroxisomal Membrane. , 2.3 Peroxisomal Import Pores.
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  • 3
    Keywords: Cytology ; Cytology ; Proteomics ; Biochemistry ; Human genetics ; Cell physiology ; Biochemistry ; Human genetics ; Cell physiology ; Proteomics ; Cell biology. ; Plant biochemistry. ; Peroxisomes ; Proteomics methods
    Description / Table of Contents: This new edited volume in the Springer Subcellular Biochemistry Series presents a comprehensive, state-of-the-art overview of the proteomics of peroxisomes derived from mammalian, Drosophila, fungal, and plant origin, andcontains contributions from leading experts in the field. The development of sensitive proteomics and mass spectrometry technologies, combined with bioinformatics approaches now allow the identification of low-abundance and transient peroxisomal proteins and permits to identify the complete proteome of peroxisomes, with the consequent increase of our knowledge of the metabolic and regulatory networks of these important cellular organelles. The book lines-up with these developments and is organized in four sections including: (i) mass spectrometry-based organelle proteomics; (ii) prediction of peroxisomal proteomes; (iii) analysis of peroxisome proteome interaction networks; and (iv) peroxisomes in relation to other subcellular compartments. The editor Luis A. del Río is Professor ad honorem of the Spanish National Research Council (CSIC) in the Group of Antioxidants, Free Radicals and Nitric Oxide in Biotechnology, Food and Agriculture, Department of Biochemistry and Cell & Molecular Biology of Plants, at the Estación Experimental del Zaidín, Granada, Spain. Del Río’s research group focuses on the metabolism of reactive oxygen species (ROS), reactive nitrogen species (RNS) and antioxidants in plant peroxisomes, and the ROS- and RNS-dependent role of peroxisomes in plant cell signalling. The editor Michael Schrader is Professor of Cell Biology & Cytopathology in the Department of Biosciences at the University of Exeter, UK. Using mammalian peroxisomes as model organelles, Prof. Schrader and his team aim to unravel the molecular machinery and signalling pathways that mediate and regulate the formation, dynamics and abundance of these medically relevant cellular compartments
    Type of Medium: Online Resource
    Pages: Online-Ressource (XIII, 493 p. 55 illus., 49 illus. in color, online resource)
    Edition: Springer eBook Collection. Biomedical and Life Sciences
    ISBN: 9789811322334
    Series Statement: Subcellular Biochemistry volume 89
    Language: English
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  • 4
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 92 (1994), S. 0 
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Superoxide dismutases (SOD; EC 1.15.1.1) in chestnut (Castanea sativa Mill., cv. 431) leaves were characterized by native polyacrylamide gel electrophoresis. The three molecular forms of SOD were distinguished from each other by their different sensitivity to cyanide and H2O2 Three CuZn-containing SODs were detected (CuZn-SOD I, II. and III), and all the isozymes had a molecular mass of 33 kDa. CuZn-SOD III was the most abundant isozyme. whereas CuZn-SOD II was present in a minor amount. In leaves showing typical symptoms of senescence increases of 2.5-. 7- and 4-fold in the specific activities of CuZn-SODs I, II, and III. respectively, were found. In addition, the pattern of the three isozymes was modified by the age of leaves, a rise in the CuZn-SOD II and a decrease in the CuZn-SOD 1 percentages being found in senescent leaves compared to green leaves. As to other activated oxygen-related enzymes, an increase in the superoxide-generating xanthine oxidase activity and a decline in both catalase and peroxidase activities during natural senescence of chestnut leaves were observed. Results obtained suggest that in natural senescence of chestnut leaves activated oxygen species are involved, and an overproduction of hydrogen peroxide and superoxide radicals probably takes place.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Copenhagen : Munksgaard International Publishers
    Physiologia plantarum 104 (1998), S. 0 
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Gametophytic tissues of plants are an area largely neglected in the broad literature on free radical processes in plants. In order to study the mechanisms of protection against oxidative stress in pollen, the presence of the key antioxidative enzyme superoxide dismutase (SOD; EC 1.15.1.1) was investigated. Crude extracts of olive tree (Olea europaea L.) pollen were subjected to native PAGE in 10% polyacrylamide gels. The SOD activity staining of gels showed the presence of four isoenzymes. All the SODS were completely inhibited by 2 mM KCN and 5 mM H2O2, and therefore belong to the family of CuZn-SODS. Isoelectric focusing (pH 3.5-7) of crude extracts and further detection of SOD activity allowed determination of isoelectric points for the four isoforms, namely 4.60, 4.78, 5.08 and 5.22. The cross-reactivity of pollen extracts with a polyclonal antibody to cytosolic CuZn-SOD from spinach leaves was assayed by western blotting. After SDS-PAGE and immunoblotting, a major polypeptide band of about 16.5 kDa was detected, which is characteristic of the subunit of most CuZn-SODS. Immunocytochemical studies at TEM level using the same antiserum showed that CuZn-SOD was localized in the cytoplasm of both vegetative and generative cells, and also in material adhered to the pollen wall. The olive pollen CuZn-SODS could function in the protection against oxidative stress during pollen development.
    Type of Medium: Electronic Resource
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  • 6
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The peroxisomal manganese superoxide dismutase (perMn-SOD; EC 1.15.1.1) was purified to homogeneity for the first time from peroxisomes of pea (Pisum sativum L.) leaves. Peroxisomes were isolated from pea leaves by sucrose density-gradient centrifugation, and then perMn-SOD was purified from these organelles by two purification steps involving anion-exchange and gel-filtration fast protein liquid chromatography. Pure peroxisomal Mn-SOD had a specific activity of 2 880 units per mg protein and was purified 3 000-fold, with a yield of about 7 µg enzyme per kg pea leaves. The relative molecular mass determined for perMn-SOD was 92 000, and it was composed of four equal subunits of 27 kDa. Ultraviolet and visible absorption spectra of the enzyme showed two absorption maxima at 278 and 483 nm, respectively, and two shoulders at 290 and 542 nm. By isoelectric focusing (pH 5-7), an isoelectric point of 5.53 was determined for perMn-SOD. In immunoblot assays, purified Mn-SOD was recognized by a polyclonal antibody against mitochondrial Mn-SOD (mitMn-SOD) from pea leaves. The amino acid sequence of the N-terminal region of the purified peroxisomal enzyme was determined. A 100% identity was found with the mitMn-SOD from pea leaves, and high identities were also found with Mn-SODs from other plant species.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Copenhagen : Munksgaard International Publishers
    Physiologia plantarum 104 (1998), S. 0 
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Peroxisomes are subcellular organelles with an essentially oxidative type of metabolism. The presence in these organelles of superoxide dismutases and the generation of superoxide radicals (O2•−) was first demonstrated in plant tissues and in recent years different experimental evidence has suggested the existence of cellular functions related to activated oxygen species. Some of these functions are analyzed in this work.In purified intact peroxisomes from pea (Pisum sativum L.) leaves, xanthine oxidase and urate oxidase were found to be present. The occurrence and the level of the metabolites xanthine, hypoxanthine, uric acid, and allantoin were studied in extracts of pea leaf peroxisomes by HPLC. Xanthine, uric acid, and allantoin were detected in peroxisomes. These results suggest a cellular role for leaf peroxisomes in the catabolism of purines.In peroxisomal membranes, 3 polypeptides (PMPs) with molecular masses of 18, 29 and 32 kDa, respectively, have been shown to generate superoxide radicals. These PMPs were purified from pea leaf peroxisomal membranes and characterized. While the 18- and 32-kDa PMPs use NADH as electron donor for O2•− production, the 29-kDa PMP was clearly dependent on NADPH.Very recently, the occurrence in pea leaf peroxisomes of all the enzymes of the ascorbate-glutathione cycle has been demonstrated. NADPH is required for the glutathione reductase activity of the cycle and this implies the reduction of NADP+ to NADPH. This recycling function could be carried out by the NADP-dependent glucose-6-phosphate dehydrogenase (G6PDH), 6-phosphogluconate dehydrogenase (6PGDH), and isocitrate dehydrogenase (ICDH). These 3 dehydrogenases have been demonstrated to be present in the matrix of pea leaf peroxisomes.The catabolism of purines, the superoxide-generating PMPs, the ascorbate-glutathione cycle, and the dehydrogenase-mediated recycling of NADPH, are activated oxygen roles of leaf peroxisomes that add to other functions previously known for peroxisomes from eukaryotic cells.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 90 (1994), S. 0 
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: An iron-containing superoxide dismutase (SOD, EC 1.15.1.1) was fully characterized from leaves of the higher plant Citrus limonum R. cv. Verna. This enzyme is the first iron-containing SOD to be characterized in the plant family Rutaceae. The purified Fe-SOD has a molecular mass of about 47 kDa and is composed of two non-covalently joined equal subunits. The amino acid composition determined for the enzyme was compared with that of a wide range of SODs and had highest degree of homology with the Fe-SODs from Brassica campestris and Nuphar luteum. The enzyme was more labile at high temperatures than some eucaryotic and procaryotic Fe-SODs. It showed a maximum stability at pH 7.8. The sensitivity of the enzyme to cyanide, hydrogen peroxide and o-phenanthroline was similar to those reported for other Fe-SODs. but the lemon enzyme was comparatively resistant to H2O2. By kinetic competition experiments, the rate constant for the disproportionation of superoxide radicals by lemon Fe-SOD was found to be 1.9 × 109M−1 s−1 at pH 7.8 and 25°C. A comparative study between the molecular properties of this higher plant Fe-SOD and SODs from different origins is presented.
    Type of Medium: Electronic Resource
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  • 9
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The effect in vivo of salt stress on the activated oxygen metabolism of mitochondria, was studied in leaves from two NaCl-treated cultivars of Pisum sativum L. with different sensitivity to NaCl. In mitochondria from NaCl-sensitive plants, salinity brought about a significant decrease of Mn-SOD (EC 1. 15. 1. 1) Cu, Zn-SOD I (EC 1. 15. 1. 1) and fumarase (EC 4. 2. 1. 2) activities. Conversely, in salt-tolerant plants NaCl treatment produced an increase in the mitochondrial Mn-SOD activity and, to a lesser extent, in fumarase activity. In mitochondria from both salt-treated cultivars, the internal H2O2 concentration remained unchanged. The NADH- and succinate-dependent generation of O2.−radicals by submitochondrial particles and the lipid peroxidation of mitochondrial membranes, increased as a result of salt treatment, and these changes were higher in NaCl-sensitive than in NaCl-tolerant plants. Accordingly, the enhanced rates of superoxide production by mitochondria from salt-sensitive plants were concomitant with a strong decrease in the mitochondrial Mn-SOD activity, whereas NaCl-tolerant plants appear to have a protection mechanism against salt-induced increased O2.− production by means of the induction of the mitochondrial Mn-SOD activity. These results indicate that in the subcellular toxicity of NaCl in pea plants, at the level of mitochondria, an oxidative stress mechanism mediated by superoxide radicals is involved, and also imply a function for mitochondrial Mn-SOD in the molecular mechanisms of plant tolerance to NaCl.
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 87 (1993), S. 0 
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The isoenzymatic pattern of Superoxide dismutase (SOD; EC 1.15.1.1) was studied in the symbiosis of Glomus mosseae (Nicol. and Gerd.) Gerd. and Trappe-Trifolium prarense L A Cu.Zn-SOD (M, 40500) was found in spores of G. mosseae. while one Mn-SOD (Mn-SOD I) and two Cu.Zn-SODs (Cu.Zn-SOD 1 and Cu.Zn-SOD II) were present in both roots and leaves of T. pratense. Molecular masses for Cu.Zn-SOD I and Cu.Zn-SOD II were 31000 and 34300. respectively. However, when T. prateme and G. mosseae were associated, mycorrhizal roots showed two new iso-zymes, Mn-SOD II and mycCu.Zn-SOD, which have relative molecular masses of 37 800 and 33 300, respectively. The mycCu.Zn-SOD was found to be specific for this association, whereas Mn-SOD II was also present in nodules of Rhizobium-T. pra-tense. Results suggest that both enzymes are induced in the T. praiense roots in response to invasion by mycorrhizal fungi, perhaps as a result of an increase in the generation of O-2 radicals in plant roots.
    Type of Medium: Electronic Resource
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