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  • 1
    ISSN: 1432-072X
    Keywords: ppGpp ; Nitrogen starvation ; Anacystis nidulans ; Cyanobacterium ; Guanosine tetraphosphate ; GTP ; ATP ; Nitrate starvation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The effect of nitrate deprivation on cell growth and nucleotide level was studied in Anacystis nidulans. A 10-fold reduction in nitrate level resulted in a drastic slowdown of growth. Upon addition of nitrate to the starving cultures, after a lag period, the cells resumed growth. Nutritional shift-down induced a transitory expansion of the guanosine tetraphosphate (ppGpp) pool, preceeded by a transitory increase in GTP and ATP concentrations. After having reached peak values, the concentration of ppGpp, GTP and ATP dropped to the respective base levels. The expansion of the ppGpp pool was found to be due to an increase in ppGpp synthesis, rather than to a decrease in ppGpp breakdown. After nutritional shift-up, no decrease in the ppGpp level was found. In starving cells, a decrease in free amino acids was observed to occur concomitantly with the expansion of the ppGpp pool. The level of free amino acids started to increase simultaneously with the contraction of the ppGpp pool.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 133 (1982), S. 2-5 
    ISSN: 1432-072X
    Keywords: Anacystis nidulans ; Cyanobacterium ; Glutathione ; Glyceraldehyde-3-phosphate dehydrogenase ; Redox modulation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.13; GAPDH) from the cyanobacteriumAnacystis nidulans was activated up to five-fold by reduced glutathione (GSH) in the physiological concentration range (0.1–2 mM GSH). Non-physiological reductants, like dithiothreitol (DTT) and β-mercaptoethanol, also activated the enzyme. Oxidized glutathione (GSSG) had no effect on the cyanobacterial GAPDH but treatment with H2O2 led to a rapid, reversible deactivation of both untreated and GSH-treated enzyme preparations. GSH reversed the inhibition induced by H2O2. An oligomeric form of the enzyme (apparentM r∼440,000) was dissociated by GSH into a lower-M r, more active enzyme form (M r∼200,000). The enzyme was shown to obey regular Michaelis-Menten kinetics. The activation of GAPDH by GSH was associated with a decrease inK m and an increase inV max values of the enzyme for 3-phosphoglycerate. GSH had virtually no effect on a GAPDH preparation isolated from corn chloroplasts and studied for comparison.
    Type of Medium: Electronic Resource
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