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  • 62G10  (1)
  • Candida boidinii  (1)
  • 1995-1999  (2)
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Georgian mathematical journal 3 (1996), S. 343-362 
    ISSN: 1572-9176
    Keywords: 62G05 ; 62G10 ; 60G10 ; Lévy random measure ; Lévy bridge ; Lévy broken bridge ; compound Poisson random measure ; change-set
    Source: Springer Online Journal Archives 1860-2000
    Topics: Mathematics
    Notes: Abstract The classical change-point problem in modern terms, i.e., the mode-change problem, is stated for sufficiently general set-indexed random processes, namely for random measures. A method is shown for solving this problem both in the general form and for the intensity of compound Poisson random measures. The results obtained are novel for the change-point problem, too.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    World journal of microbiology and biotechnology 14 (1997), S. 191-197 
    ISSN: 1573-0972
    Keywords: Candida boidinii ; catalase ; electron microscopy ; methanol-utilizing yeasts ; mitochondria
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Catalase activity of the methanol-assimilating yeast Candida boidinii M-363 was determined cytochemically and biochemically. Electron microscopic investigations on ultrathin sections were made on cells from 16, 24, and 48h batch cultures in nutrient medium with methanol (or glucose as a control) as the sole source of carbon and energy. The electron-dense oxidation product of 3,3′-diaminobenzidine was found predominantly in the mitochondrial cristae and membranes. The mitochondria were increased in number, enlarged, sometimes aggregated, with variable form and size and they characteristically developed when the strain was grown on methanol. The significant development of these organelles and their intensive DAB staining correlated with the considerable increase in catalase activity. Biochemically, catalase in the cell-free extract was determined to be maximal along the exponential growth phase of the strain during its incubation on methanol. Enzyme analysis of the heavy mitochondrial fraction showed that it possessed catalase activity but not peroxidase activity. The results showed that not only peroxisomes but also mitochondria may be structurally and functionally responsible for the high catalase activity of some methanol-assimilating yeasts. What is more, the contribution of the mitochondria to the utilization of methanol may be significant.
    Type of Medium: Electronic Resource
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