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  • 1990-1994  (4)
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  • 1
    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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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Superoxide dismutase in vesicular arbuscular-mycorrhizal red clover plants (1993)
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 87 (1993), S. 0 
    Details
    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
    URL: http://dx.doi.org/10.1111/j.1399-3054.1993.tb08793.x
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  • 3
    Electronic Resource
    Electronic Resource
    Subcellular distribution of superoxide dismutase in leaves of ureide-producing leguminous plants (1991)
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 82 (1991), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The subcellular localization of superoxide dismutase (SOD; EC. 1.15.1.1) was studied in leaves of two ureide-producing leguminous plants (Phaseolus vulgaris L. cv. Contender and Vigna unguiculata [L.] Walp). In leaves of Vigna and Phaseolus, three superoxide dismutases were found, an Mn-SOD and two Cu, Zn-containing SODs (I and II). Chloroplasts, mitochondria, and peroxisomes were purified by differential and density-gradient centrifugation using either Percoll or sucrose gradients. The yields obtained in intact chloroplasts and peroxisomes from Vigna were considerably higher than those achieved for Phaseolus. Purified chloroplasts only contained the Cu, Zn-SOD II isozyme, but in mitochondria both Mn-SOD and Cu, Zn-SOD I isozymes were present. In purified peroxisomes no SOD activity was detected. The absence of SOD activity in leaf peroxisomes from Vigna contrasts with results reported for the amide-metabolizing legume Pisum sativum L. where the occurrence of Mn-SOD was demonstrated in leaf peroxisomes (del Río et al. 1983. Planta 158: 216–224; Sandalio et al. 1987. Plant Sci. 51: 1–8). This suggests that in leaf peroxisomes from Vigna plants the generation of O2- radicals under normal conditions probably does not take place.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1399-3054.1991.tb00095.x
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  • 4
    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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