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  • 1
    ISSN: 1432-0789
    Keywords: Anabaena ; Artificial association ; Cyanobacteria ; Nostoc ; Polysaccharide ; Root association Wheat
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Geosciences , Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Abstract The characteristics of the mucilaginous sheaths of the cyanobacteria Nostoc 2S9B and Anabaena C5 and their role in the formation of associations with the roots of wheat plants grown in liquid culture have been assessed. Light and scanning electron microscopy revealed that the filaments of Nostoc 2S9B that formed a tight association with the root surface were contained in a firm mucilaginous shell. In contrast, filaments of Anabaena C5 formed a loose association and were easily detached from the mucilage that had a sheet-like appearance and tended to disintegrate as the culture aged. Similarly, there was a tight attachment of the isolated polysaccharide from Nostoc 2S9B to the root surface and a loose attachment of the Anabaena C5 polysaccharide. When the crude polysaccharide from Nostoc 2S9B was freed from proteins by phenol or pronase treatment, its ability to adhere to the root surface was lost or considerably reduced, suggesting that a protein component contributes to the tight attachment of Nostoc 2S9B. The crude polysaccharide preparation from Nostoc 2S9B contained 2.8% (w/w) protein while that from Anabaena C5 was only 0.6% (w/w) protein. The purified exopolysaccharide from Nostoc 2S9B contained three neutral sugars and glucuronic acid, whereas fucose and a uronic acid were the main components of that from Anabaena C5. Washing the roots or treating them with different sugars did not alter the ability of Nostoc 2S9B to colonize the root surface, indicating that cyanobacterial attachment may not be specific.
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  • 2
    ISSN: 1432-0789
    Keywords: Anabaena ; Cyanobacteria ; Nitrogenase activity (acetylene reduction assay) ; Nostoc ; Symbiosis ; Triticum vulgare ; Wheat
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Geosciences , Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Summary Following co-cultivation of wheat with N2-fixing cyanobacterial isolates capable of forming associations, Nostoc 2S6B, 2S9B or Anabaena C5, for 15 days in the presence or absence of combined N a large stimulation of root length was observed without any increase in root dry weight. Increases in the N concentrations of both roots and shoots occurred following co-cultivation with most cyanobacteria tested. The increase in plant N concentrations appeared to be dependent on the wheat cultivar and the cyanobacterial isolate used. Nostoc isolates had similar nitrogenase activities when associated with roots and when grown in shake-flask cultures. The nitrogenase activity of roots colonized by Anabaena C5 or Nostoc 2S6B was higher following removal of loosely associated cyanobacteria.
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  • 3
    ISSN: 1432-072X
    Keywords: Ammonia assimilation ; Lichen symbioses ; Nitrogen fixation ; 15N kinetics ; Peltigera canina
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract On following N2-incorporation and subsequent metabolism in the lichen Peltigera canina using 15N as tracer, it was found, over a 30 min period, that greatest initial labelling was into NH 4 + followed by glutamate and the amide-N of glutamine. Labelling of the amino-N of glutamine, aspartate and alanine increased slowly. Pulse-chase experiments using 15N confirmed this pattern. On inhibiting the GS-GOGAT pathway using l-methionine-dl-sulphoximine and azaserine, 15N enrichment of glutamate, alanine and aspartate continued although labelling of glutamine was undetectable. From this and enzymic data, NH 4 + assimilation in the P. canina thallus appears to proceed via GS-GOGAT in the cyanobacterium and via GDH in the fungus; aminotransferases were present in both partners. The cyanobacterium assimilated 44% of the 15N2 fixed; the remainder was liberated almost exclusively as NH 4 + and then assimilated by fungal GDH.
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 143 (1986), S. 353-358 
    ISSN: 1432-072X
    Keywords: Ammonium transport ; Cyanobacteria ; Glutamine synthetase ; Methionine sulphoximine ; Methylammonium transport
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The cyanobacteria Anabaena variabilis and Nostoc CAN showed a biphasic pattern of 14CH3NH 3 + uptake at external pH values of 7.0 and 9.0. The initial phase of uptake, which was independent of metabolism of 14CH3NH 3 + , was attributed to uptake via a CH3NH 3 + (NH 4 + ) transport system at pH 7.0 and probably to passive diffusion of uncharged CH3NH2 and trapping by protonation at pH 9.0. The second slower phase of uptake was attributed to metabolism of CH3NH 3 + via glutamine synthetase to form γ-methylglutamine which accumulates. Anabaena cylindrica showed an initial rapid uptake at pH 7.0 and pH 9.0 but metabolism of 14CH3NH 3 + was undetectable at pH 7.0 and was barely detectable at pH 9.0. Pretreatment of A. variabilis with l-methionine-d,l-sulphoximine to inactivate glutamine synthetase, inhibited the second phase of 14CH3NH 3 + uptake at both pH 7.0 and pH 9.0 and the accumulation of γ-methylglutamine but had no effect on the first phase of uptake. Following transfer of A. variabilis to darkness the initial phase of 14CH3NH 3 + uptake at pH 7.0 and 9.0 was unaffected but the subsequent metabolism via glutamine synthetase was inhibited.
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  • 5
    ISSN: 1432-072X
    Keywords: Amino acid liberation ; Anabaena variabilis ; Aromatic amino acid biosynthesis ; Cyanobacteria ; DAHP synthase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Mutant strains of Anabaena variabilis which are resistant to the tryptophan analogue, 6-fluorotryptophan, liberated a wide range of amino acids although none liberated tryptophan in detectable quantities. Four strains (FT-7, FT-8, FT-9, FT-10) produced predominantly alanine together with small amounts of phenylalamine and tyrosine, strain FT-2 liberated mainly phenylalanine and tyrosine and strain FT-6 liberated mainly glutamate, NH 4 + and several unidentified ninhydrin-positive compounds. Two forms of 3-deoxy-D-arbinoheptulosonate 7-phosphate (DAHP) synthase were identified in the parent strain, a tyrosine-sensitive form and a phenylalanine-sensitive form. In strains FT-2 and FT-6 the phenylalanine-sensitive enzyme was not detected and in strain FT-7 it was apparently deregulated with respect to inhibition by phenylalanine. No deregulation of anthranilate synthase was observed but mutant strains were found to have higher specific activities of this enzyme than the parent strain.
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  • 6
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 137 (1984), S. 241-246 
    ISSN: 1432-072X
    Keywords: Ammonium transport ; Anabaena azollae ; Anabaena variabilis ; Cyanobacteria ; Methylammonium transport ; Symbiosis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The free-living cyanobacterium Anabaena variabilis showed a biphasic pattern of 14CH3NH 3 + uptake. Initial accumulation (up to 60 s) was independent of CH3NH 3 + metabolism, but long-term uptake was dependent on its metabolism via glutamine synthetase (GS). The CH3NH 3 + was converted into methylglutamine which was not further metabolised. The addition of l-methionine-dl-sulphoximine (MSX), to inhibit GS, inhibited CH3NH 3 + metabolism, but did not affect the CH3NH 3 + transport system. NH 4 + , when added after the addition of 14CH3NH 3 + , caused the efflux of free CH3NH 3 + ; when added before 14CH3NH 3 + , NH 4 + inhibited its uptake indicating that both NH 4 + and CH3NH 3 + share a common transport system. Carbonylcyanide m-chlorophenylhydrazone and triphenyl-methylphosphonium both inhibited CH3NH 3 + accumulation indicating that the transport system was Δψ-dependent. At pH 7 and at an external CH3NH 3 + concentration of 30 μmol dm-3, A. variabilis showed a 40-fold intracellular accumulation of CH3NH 3 + (internal concentration 1.4 mmol dm-3). Packets of the symbiotic cyanobacterium Anabaena azollae, directly isolated from the water fern Azolla caroliniana, also showed a Δψ-dependent NH 4 + transport system suggesting that the reduced inhibitory effect of NH 4 + on nitrogenase cannot be attributed to the absence of an NH 4 + transport system but is probably related to the reduced GS activity of the cyanobiont.
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 141 (1985), S. 244-248 
    ISSN: 1432-072X
    Keywords: Ammonia analogues ; Anabaena variabilis ; Cyanobacteria ; Ethylenediamine ; Nitrogen fixation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The cyanobacterium Anabaena variabilis showed a pH dependent uptake of ethylenediamine. No uptake of ethylenediamine was detected at pH 7.0. At higher pH values (e.g. pH 8.0 and pH 9.0) accumulation did occur and was attributed to diffusion of uncharged ethylenediamine in response to a pH gradient. A biphasic pattern of uptake was observed at these higher pH values. Treatment with l-methionine-d,l-sulphoximine (MSX) to inactivate glutamine synthetase (GS) inhibited the second slower phase of uptake without any significant alteration of the initial uptake. Therefore for sustained uptake, metabolism of ethylenediamine via GS was required. NH 4 + did not alter the uptake of ethylenediamine. Ethylenediamine was converted in the second phase of uptake to an analogue of glutamine which could not be detected in uptake experiments at pH 7.0 or in uptake experiments at pH 9.0 following pretreatment of cells with MSX. Ethylenediamine treatment inhibited nitrogenase activity and this inhibition was greatest at high pH values.
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  • 8
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Levels of glutamine synthetase (GS) biosynthetic activity, GS protein and GS mRNA were compared in the parent strain of Anabaena variabilis and in ammonia-liberating mutant strains (ED81 and ED92) which are resistant to ethylenediamine (EDA). GS activity, protein and mRNA levels were all reduced in ED92 whereas ED81 had levels of GS protein and mRNA similar to those of the parent strain but had much reduced GS biosynthetic activity. These findings are discussed in relation to the type of mutation occurring within in each mutant strain and in relation to the reduced GS activity in the Anabaena-Azolla symbiotic association.
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  • 9
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Journal of medicinal chemistry 19 (1976), S. 300-303 
    ISSN: 1520-4804
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
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  • 10
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 57 (1983), S. 0 
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Acetylene reduction (nitrogenase activity) by excised cephalodia of Peltigera aphthosa Willd. slowly declined on transfer of the cephalodia from light to darkness. The decline was more rapid in the absence of CO2 or when phosphoenolpyruvate carboxylase activity was inhibited by adding maleic acid or malonic acid. When glutamine synthetase (GS) activity was totally inhibited by adding l-methionine-dl-sulphoximine (MSX) the decline in nitrogenase activity in the absence of CO2 still occurred. However, this loss of activity did not occur when the mycobiont was disrupted using digitonin (0.01 % w/v) and the fixed NH4+ was released into the medium. The data suggest that dark CO2 fixation by the fungus supplies carbon skeletons which remove newly fixed NH4+ produced by the cyanobacterium. When such carbon skeletons are not available MH4+ accumulates and inhibits nitrogenase activity even in the absence of GS activity. It is probable that NH4+ and a product of GS exert independent inhibitory effects on nitrogenase activity.
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