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  • 1
    Electronic Resource
    Electronic Resource
    Tellurium-related trap levels in silicon (1984)
    Springer
    Applied physics 33 (1984), S. 19-24 
    Details
    ISSN: 1432-0630
    Keywords: 61.70lm ; 71.55Fr
    Source: Springer Online Journal Archives 1860-2000
    Topics: Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Notes: Abstract Tellurium-related defects inn-type silicon have been analysed by deep level transient spectroscopy (DLTS). The tellurium doping of the samples was performed by ion implantation or during epitaxy. In all the samples, a level having a thermal activation energy around 0.37 eV is observed. This activation energy is found to be dependent on the electric field. Taking into account the Poole-Frenkel (FP) effect and a temperature dependence proportional toT −2 in the capture cross-section, a value ofE A=0.41eV is obtained. A second Te-related level having an activation energy ofE A=0.14eV without correction of the FP effect could only be measured in the implanted samples. The same concentration is observed for the two levels in the implanted samples thus indicating that both peaks in the DLTS spectra are caused by the identical Te-related defect.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01197080
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Cyclic AMP, fructose-2,6-bisphosphate and catabolite inactivation of enzymes in the hydrocarbon-assimilating yeast Candida maltosa (1989)
    Springer
    Archives of microbiology 152 (1989), S. 269-272 
    Details
    ISSN: 1432-072X
    Keywords: Candida maltosa ; catabolite inactivation ; Cyclic AMP ; Fructose-2,6-bisphosphate
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The inactivation of fructose-1,6-bisphosphatase, isocitrate lyase and cytoplasmic malate dehydrogenase in Candida maltosa was found to occur after the addition of glucose to starved cells. The concentration of cyclic AMP and fructose-2,6-bisphosphate increased drastically within 30 s when glucose was added to the intact cells of this yeast. From these results it was concluded that catabolite inactivation, with participation of cyclic AMP and fructose-2,6-bisphosphate, is an important control mechanism of the gluconeogenetic sequence in the n-alkane-assimilating yeast Candida maltosa, as described for Saccharomyces cerevisiae.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00409662
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Characterization of a mutant of the yeast Candida maltosa defective in catabolite inactivation of gluconeogenetic enzymes (1990)
    Springer
    Archives of microbiology 154 (1990), S. 514-517 
    Details
    ISSN: 1432-072X
    Keywords: Candida maltosa ; Mutant ; Pseudohyphal morphology ; Glucose uptake ; Cyclic AMP ; Catabolite inactivation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A spontaneous mutant of the yeast Candida maltosa SBUG 700 was isolated showing pseudohyphal marphology under all growth conditions tested. The C. maltosa PHM mutant takes up glucose with the kinetics of C. maltosa SBUG 700 and starved cells contain the same cyclic AMP concentration. Addition of glucose to the PHM mutant does not result in an increase of the intracellular cyclic AMP level and in catabolite inactivation of fructose-1,6-bisphosphatase, malate dehydrogenase and phosphoenolpyruvate carboxykinase. However, addition of 2,4-dinitrophenol is followed by a rapid, transient increase of the cyclic AMP level in the mutant cells, but not by catabolite inactivation. These results show that a common mechanism might be responsible for catabolite inactivation and glucose-induced cAMP signaling or that glucose-induced cAMP signaling is required for catabolite inactivation in C. maltosa.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00245237
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    Paper (German National Licenses)
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