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  • 11
    Electronic Resource
    Electronic Resource
    Activated oxygen-mediated metabolic functions of leaf peroxisomes (1998)
    Copenhagen : Munksgaard International Publishers
    Physiologia plantarum 104 (1998), S. 0 
    Details
    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
    URL: http://dx.doi.org/10.1034/j.1399-3054.1998.1040422.x
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  • 12
    Electronic Resource
    Electronic Resource
    Superoxide dismutases of chestnut leaves, Castanea sativa: Characterization and study of their involvement in natural leaf senescence (1994)
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 92 (1994), S. 0 
    Details
    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
    URL: http://dx.doi.org/10.1111/j.1399-3054.1994.tb05330.x
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  • 13
    Electronic Resource
    Electronic Resource
    Proteolytic cleavage of plant proteins by peroxisomal endoproteases from senescent pea leaves (1999)
    Springer
    Planta 209 (1999), S. 308-313 
    Details
    ISSN: 1432-2048
    Keywords: Key words: Peroxisome ; Pisum (senescence) ; Proteolysis ; Ribulose-1 ; 5 ; -bisphosphate carboxylase/oxygenase ; Senescence ; Xanthine oxidase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract. The degradation of peroxisomal and nonperoxisomal proteins by endoproteases of purified peroxisomes from senescent pea (Pisum sativum L.) leaves has been investigated. In our experimental conditions, most peroxisomal proteins were endoproteolytically degraded. This cleavage was prevented, to some extent, by incubation with 2 mM phenylmethylsulfonylfluoride, an inhibitor of serine proteinases. The peroxisomal enzymes glycolate oxidase (EC 1.1.3.1), catalase (EC 1.11.1.6) and glucose-6-phosphate dehydrogenase (EC 1.1.1.49) were susceptible to proteolytic degradation by peroxisomal endoproteases, whereas peroxisomal manganese superoxide dismutase (EC 1.15.1.1) was not. Ribulose-1,5-bisphosphate carboxylase/oxygenase (EC 4.1.1.39) from spinach and urease (EC 3.5.1.5) from jack bean were strongly degraded in the presence of peroxisomal matrices. These results indicate that proteases from plant peroxisomes might play an important role in the turnover of peroxisomal proteins during senescence, as well as in the turnover of proteins located in other cell compartments during advanced stages of senescence. On the other hand, our data show that peroxisomal endoproteases could potentially carry out the partial proteolysis which results in the irreversible conversion of xanthine dehydrogenase into the superoxide-generating xanthine oxidase (EC 1.1.3.22). This suggests a possible involvement of the peroxisomal endoproteases in a regulated modification of proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004250050637
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  • 14
    Electronic Resource
    Electronic Resource
    Protein patterns and superoxide dismutase activity in non-mycorrhizal and arbuscular mycorrhizalPisum sativum L. plants (1994)
    Springer
    Plant and soil 166 (1994), S. 37-45 
    Details
    ISSN: 1573-5036
    Keywords: arbuscular mycorrhizal fungi ; isozymes ; nodules ; Pisum sativum ; proteins ; superoxide dismutase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Abstract There are few reports in relation to the role of specific proteins in the mycorrhizal symbiosis. Among the changes in the protein expression as a consequence of the arbuscular mycorrhizal symbiosis, only one case related to changes in superoxide dismutase (SOD; EC 1.15.1.1) activity has been reported in the red clover-Glomus mosseae symbiosis. In this paper, the symbiotic system formed by a leguminous plant,Pisum sativum, and the fungusGlomus mosseae is studied in terms of protein patterns and SOD activity in both mycorrhizal and non-mycorrhizal roots. Our results show that among the differential polypeptides separated by SDS-PAGE, one with a molecular weight of 32.0 kDa, and a protein with an isoelectric point of pI 4.9 appeared strongly expressed in mycorrhizal roots. A partial purification of the related polypeptide could be achieved by DEAE-cellulose chromatography. A higher SOD activity was also detected in mycorrhizal pea roots, although both mycorrhizal and non-mycorrhizal roots showed the same isoenzymatic pattern for SODs: two Mn-SODs (I and II) and two Cu,Zn-SODs (I and II) were detected, Cu,Zn-SOD I being the most abundant isozyme in both types of roots. A similar pattern of SOD isozymes (Mn-SODs I and II, and Cu,Zn-SODs I and II) was also found in nodules of mycorrhizal and non-mycorrhizal pea roots. However, in nodules Mn-SOD II was the main isozyme. The bacterial nature of this isozyme is postulated in this report.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02185479
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