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  • 1
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Biochemistry 1 (1962), S. 189-191 
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Naturwissenschaften 10 (1922), S. 46-47 
    ISSN: 1432-1904
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Natural Sciences in General
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Naturwissenschaften 10 (1922), S. 925-925 
    ISSN: 1432-1904
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Natural Sciences in General
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  • 5
    ISSN: 1432-1211
    Keywords: Key words Vβ13 ; CD4/CD8 ratio ; Rat ; Tcrb ; Polymorphism
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. Three rat BV13S1 alleles (T-cell receptor β-chain variable gene 13) were characterized by new BV13S1-allele specific monoclonal antibodies (18B1 and 17D5) and sequence analysis of expressed and genomic BV13S1. Two alleles were functional and designated BV13S1A1 present in strains LEW, BUF, PVG, and BV13S1A2 present in BN and WF. Their products differed by six amino acids, two of them in complementarity-determing region (CDR)1 and one in CDR2. A third nonfunctional allele, BV13S1A3P, was found in strains F344 and DA. Apart from a single nucleotide insertion, it was identical to BV13S1A2. All 12 rat strains tested showed association of TCRBC1 with BV8S2/4 alleles but not with the BV13S1 alleles, which may reflect a different gene order of the rat BV compared to mouse. BV13S1A1-encoded T-cell receptors (TCRs) which bind both monoclonal antibody (mAb) 18B1 and mAb 17D5 are over-represented in the CD4 lymphocyte subset. BV13S1A2-encoded TCRs which are stained by mAb 18B1 but not by mAb 17D5 show a slight CD8-biased expression. Preferential usage of BV13S1A1-positive TCRs by CD4 but not by CD8 cells in (LEW×WF)F1 hybrids and cosegregation of BV13SA1 and increased frequency of BV13S1 TCR-positive CD4 cells in a (LEW×BN)×BN backcross suggest structural differences of the two allelic products as the reason for their contrasting CD4/CD8 subset bias.
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  • 6
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 154 (1990), S. 514-517 
    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.
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 152 (1989), S. 269-272 
    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.
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  • 8
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 132 (1982), S. 179-184 
    ISSN: 1432-072X
    Keywords: Assimilation ; Methanol ; Glycerol ; Yeasts ; Dihydroxyacetone kinase ; Regulatory properties
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Fifteen yeast strains of the genera Candida, Lodderomyces, Endomycopsis, Saccharomyces, Hansenula, Pichia and Torulopsis were investigated with respect to their ability to grow on methanol, glycerol and glucose as sole carbon and energy source. Eight of them can grow on both methanol and glycerol. Methanol is assimilated via triosephosphate (dihydroxyacetone) pathway. The dihydroxyacetone kinase is a key enzyme in methanol metabolism. The assimilation of glycerol can take place in bacteria via a phosphorylative or/and oxidative pathways. In general, the phosphorylative pathway is found in eucaryotes. In the present paper it is shown that in yeasts, which can utilize methanol and glycerol, too, glycerol is assimilated via an oxidative pathway, Dihydroxyacetone is a central intermediate in the assimilation of methanol as well as glycerol. It is metabolized by means of the dihydroxyacetone kinase. The enzyme formed during growth of Candida methylica on methanol does not differ from that of Candida valida H 122 after growing on glycerol as far as the regulatory properties are concerned.
    Type of Medium: Electronic Resource
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  • 9
    ISSN: 1432-1017
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Physics
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    Springer
    European biophysics journal 8 (1981), S. 95-105 
    ISSN: 1432-1017
    Keywords: Rhodopsin ; Light-scattering ; Flash-photometry ; Disc membrane ; Rod outer segments
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Physics
    Notes: Abstract The axial and radial shrinkage of bovine rod outer segments, monitored by near-infrared scattering changes (P-signal), is investigated in dependence on the intensity of the activating flash. Suspensions of axially oriented and randomly oriented rod outer segments were measured. In the latter case, axial and radial effects are superimposed to another. The following results are obtained: 1. The axial signal (P a, Τ≈10 ms) and the radial signal (P r, Τ=40–100 ms), simultaneously measured on axially oriented rod outer segments, are similarly saturated with a half-saturation at a rhodopsin turnover of 3.5%. 2. For the saturation of the signal amplitude, measured on randomly oriented rod outer segments, a good fit is obtained by: $$\begin{gathered} P\left( \varrho \right) \sim 1 - e\beta \varrho , \hfill \\ \varrho : relative rhodopsin turnover by the flash; \hfill \\ \beta is found in the range 23 \leqslant \beta \leqslant 27 in all measurements \hfill \\ \end{gathered} $$ 3. The kinetics of the signal, also measured on the isotropic sample, depends on the rhodopsin turnover, the apparent time constant becoming faster with increasing turnover. The distortion of the signal cannot be fitted by a sum of exponentials with a fixed set of time constants. The signals from the isotropic sample are fitted by a phenomenological model. It introduces three first order processes concatenated in series; the first step is assumed as a rhodopsin transition inducing the two further processes. The distortion of the signals with increasingϱ is then described assuming aϱ-dependent quenching of this induction, according to the measured amplitude saturation. The time constants remain thereby unchanged. The fit yields the values ln 2/k=4, 11, and 45 ms with mean square deviations of 20%.
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