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  • Books
  • Articles  (3)
  • Chemical Engineering
  • Electronic structure and strongly correlated systems
  • Saccharomyces cerevisiae
  • Springer  (3)
  • 1975-1979  (3)
  • 1975  (3)
Collection
  • Books
  • Articles  (3)
Keywords
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  • 1975-1979  (3)
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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 105 (1975), S. 187-192 
    ISSN: 1432-072X
    Keywords: Peroxisomes (microbodies) ; Saccharomyces cerevisiae ; Catalase ; Urate oxidase ; Glyoxylate cycle
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Peroxisomes were isolated from derepressed (lactose grown) Saccharomyces cerevisiae cells following homogenization with a “Merkenschlager” cell mill (at 0°C using glass beads). Catalase and urate oxidase, along with low activities of d-amino acid oxidase and l-α-hydroxyacid oxidase (glycollate oxidase), were associated with the peroxisomes. No catalase activity was present in glucose repressed cells. When protoplasts prepared from derepressed cells were used for peroxisome isolation, catalase activity was not sedimentable through gradients. Apparently peroxisomes were destroyed as the cells became fermentative during protoplast preparation. The distribution of glyoxylate cycle enzymes was examined. Isocitrate lyase was not sedimentable, suggesting that, if the enzyme is peroxisome-associated, it is either readily released or present in a labile second class of peroxisomes. Low activities of malate dehydrogenase and citrate synthetase were found in peroxisome fractions from gradients, but may represent mitochondrial contamination. Citrate synthetase was not found associated with a low-density particle as had been previously reported.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 104 (1975), S. 23-28 
    ISSN: 1432-072X
    Keywords: Saccharomyces cerevisiae ; Yeast ; Chemostat ; Nutrient Concentration ; Thermal Death ; Thermal Association ; Optimum Temperature for Growth ; Maximum Temperature for Growth ; Microbial Ecology
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Saccharomyces cerevisiae was grown in a chemostat under glucose limitation at three superoptimal temperatures. In each steady state the specific growth rate was the sum of the dilution rate and the specific death rate, exponential death concurring with exponential growth. The specific death rate was a function of the temperature while the specific growth rate was a function of both the temperature and the concentration of the limiting nutrient. Each superoptimal temperature was characterized by a critical glucose concentration below which net growth was not possible. The critical glucose concentration increased with the temperature. Consequently the maximum temperature for growth was a function of the concentration of the limiting nutrient and approached the optimum temperature for growth with decreasing glucose concentrations.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 106 (1975), S. 271-273 
    ISSN: 1432-072X
    Keywords: Saccharomyces cerevisiae ; Baker's yeast ; Gluconeogenetic enzymes ; Chemostat ; Oxygen
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract 1. The effect of aeration on the key enzymes of gluconeogenesis was studied in baker's yeast (Saccharomyces cerevisiae) and in a nonrespiratory variant of S. cerevisiae grown under glucose limitation. 2. In baker's yeast phosphoenolpyruvate carboxykinase, hexosediphosphatase and isocitrate lyase were completely repressed under anaerobic conditions. Their repression could be partially reversed by using intense aeration. 3. In the nonrespiratory variant these enzymes were absent independently of aeration. 4. Pyruvate carboxylase of baker's yeast showed maximal activity under anaerobic conditions. In the nonrespiratory variant pyruvate carboxylase had low activity under both anaerobic and aerobic conditions.
    Type of Medium: Electronic Resource
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