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  • cyanobacterium  (2)
  • 1990-1994  (2)
  • 1985-1989
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Verlag/Herausgeber
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  • 1990-1994  (2)
  • 1985-1989
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  • 1
    Digitale Medien
    Digitale Medien
    Springer
    BioMetals 5 (1992), S. 149-156 
    ISSN: 1572-8773
    Schlagwort(e): Hg2+ toxicity ; cyanobacterium ; Nostoc calcicola ; growth ; photopigments ; nucleic acids ; photosynthesis ; membrane integrity ; nutrient uptake ; enzymes
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Chemie und Pharmazie
    Notizen: Abstract Toxicological responses of the filamentous N2-fixing cyanobacteriumNostoc calcicola Bréb. towards Hg2+ were studied to enumerate the decisive lethal events. In low-dose, long-term experiments (0.05–0.25 μm Hg2+, 10 days), photoautotrophic growth was severely inhibited with concurrent loss of photosynthetic pigments (phycocyanin〉chlorophyll α〉carotenoids) and nucleic acids. The termination of growth after a day 4 exposure to 0.25 μm Hg2+ has been attributed to the complete inhibition ofin vivo photosynthetic activity in the cyanobacterium (O2 evolution〉14CO2 incorporation). The elevated Hg2+ concentrations irreversibly damaged the cell membrance as observed under light microscopy, and as indicated by the leakage of intracellular electrolytes and phycocyanin. In high-dose, short-term experiments (0.5–20.0 μm Hg2+, up to 6 h), thein vivo activities of selected enzymes (glutamine synthetase 〉 nitrate reductase 〉 nitrogenase) were less inhibited by Hg2+ than the uptake of nutrient ions (NH 4 + 〉NO 3 − 〉PO 4 3− ).
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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  • 2
    Digitale Medien
    Digitale Medien
    Springer
    World journal of microbiology and biotechnology 10 (1994), S. 191-193 
    ISSN: 1573-0972
    Schlagwort(e): Anabaena cycadeae ; arginine ; cyanobacterium ; glutamine synthetase ; nitrate reductase
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Werkstoffwissenschaften, Fertigungsverfahren, Fertigung
    Notizen: Abstract Wild-type Anabaena cycadeae with normal glutamine synthetase (GS) activity utilized arginine as sole N source whereas a mutant strain lacking GS activity did not. Nitrate reductase (NR) activity, higher in the mutant strain than the wild-type strain, was inhibited by arginine though arginine-dependent NH 4 + generation was higher in the mutant strain than in the wild-type. This suggests that (1) NR activity is NO inf3 sup- -inducible and arginine-repressible; and (2) while GS activity is required for the assimilation of arginine as sole N-source, it is not required for arginine inhibition of NR activity.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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