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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 80 (1991), S. 0 
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract: Superoxide dismutase (SOD) activity was assayed in vegetative cells, heterocysts and akinetes of Anabaena cylindrica Lemm. The iron-containing isoenzyme (Fe-SOD) was in all cases predominant over the manganese-containing isoenzyme (Mn-SOD). Differentiated cells maintained the same relative content of the two enzymes as in vegetative cells. However, heterocysts and akinetes contained only 20 and 35%, respectively, of the total SOD activity present in vegetative cells.Both Mn-SOD and Fe-SOD activities increased in all types of cells isolated from A. cylindrica grown at high light intensity. The increase of SOD in heterocysts paralleled that of nitrogenase, suggesting a role of SOD in the protection mechanism of nitrogenase.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 47 (1991), S. 918-927 
    ISSN: 1600-5740
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1432-2048
    Keywords: Anabaena ; Heterocyst ; Iron-superoxide dismutase (immunogold labeling)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Iron superoxide dismutase (Fe-SOD; EC 1.15.1.1) was isolated from the nitrogen-fixing cyanobacterium Anabaena cylindrica Lemm. Polyacrylamide gel electrophoresis separated the purified protein into three closely running, enzymatically active bands. The molecular weight of the enzyme was estimated by gel filtration to be about 40 kDa. Polyclonal antibodies were produced by immunization of rabbits with the isolated enzyme, and were purified on a column of protein A-Sepharose. The Fe-SOD antibody reacted with the purified Fe-SOD and also specifically recognized the protein in extracts of A. cylindrica. In the extracts, anti-Fe-SOD did not cross-react with Mn-SOD, an enzyme which belongs to an SOD class displaying high homology of primary and three-dimensional structure with respect to Fe-SOD. Iron superoxide dismutase was localized in heterocysts by immunogold labeling and transmission electron microscopy. These results are the first in-situ evidence for the presence of SOD in the cells specialized for nitrogenase activity.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1615-6102
    Keywords: Immunogold labeling ; Iron-superoxide dismutase ; Cyanobiont ; Azolla filiculoides ; Heterocysts ; Nitrogenase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Immunogold labeling and transmission electron microscopy were used to localize iron-superoxide dismutase (Fe-SOD) in the different cells of nitrogen-fixing cyanobacterial symbiont present within different leaf cavity groups ofAzolla filiculoides Lam. As evidenced by Western blotting and immunoprecipitation, Fe-SOD antibody fromAnabaena cylindrica recognized Fe-SOD in extracts of the cyanobiont and showed the same electrophoretic mobility and pattern as purifiedA. cylindrica Fe-SOD. In vegetative cells of the cyanobiont, Fe-SOD was mainly localized in the thylakoidal membranes and in the outer membrane. The labeling pattern was similar in vegetative cells of the various groups of leaf cavities examined except at the apex where a lower gold particle density was seen. In heterocysts of the leaf cavity groups containing high nitrogenase activity, Fe-SOD labeling was most pronounced and more intense than in vegetative cells. The Fe-SOD label was preferentially located throughout the heterocyst cytoplasm and in the honeycomb regions. In accordance with the decline in nitrogenase activity, the Fe-SOD gold particle density decreased significantly in heterocysts of basal leaf cavity group. The presence of Fe-SOD in regions of high nitrogenase protein levels, and the fact that the pattern of Fe-SOD label parallels that of nitrogenase activity support a role of Fe-SOD in the protection of nitrogenase against superoxide radicals.
    Type of Medium: Electronic Resource
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