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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Journal of cancer research and clinical oncology 113 (1987), S. 298-300 
    ISSN: 1432-1335
    Keywords: Ehrlich ascites tumor cells ; DNA over-replication ; Anaerobiosis ; G2M phase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary G2-enriched fractions of Ehrlich ascites tumor cells (up to 80%–85% G2 cells) separated from anaerobically and aerobically cultured asynchronous populations by centrifugal elutriation revealed the same growth characteristics after recultivation under standard conditions: a significant proportion of cells with increased DNA (DNA content〉4C) emerged. Interruption of DNA synthesis by deprivation of oxygen may account for polyploidisation (over-replication) of DNA but other mechanisms must be taken into consideration.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-1335
    Keywords: Ehrlich ascites tumor cells ; Methylglyoxal ; Glucosone ; Galactosone ; Growth inhibition ; DNA synthesis ; Protein Synthesis ; Energy Metabolism
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary 1. Proliferation of in vitro grown Ehrlich ascites tumor cells is completely inhibited by 0.2–0.4 mM methylglyoxal and 1–2mM glucosone or galactosone without severely affecting viability (dye exclusion test); no phase-specific arrest of cell growth is observed. 2. Incorporation of [14C] thymidine into the acid-insoluble fraction of the cells decreases within a few minutes to less than 50% of that in controls in the presence of 0.4 mM methylglyoxal, and 2 mM glucosone or galactosone causes a comparable inhibition of DNA synthesis after 2 h or 4 h, respectively. 3. The action of 0.4 mM methylglyoxal inhibits incorporation of [14C] leucine within a few minutes by more than 70%, while 2 mM glucosone and galactosone are significantly less effective (50%–60% inhibition after 12 h). 4. While methylglyoxal and galactosone do not severely affect lactate production of the cells, 2 mM glucosone reduces glycolysis by 60%–70%; ATP/ADP ratios did not fall below 3.5 in the presence of the inhibitors (controls 4–6). 5. It is suggested that the reaction potentialities of the oxaldehyde function of the inhibitors play an important role in their growth-inhibitory acitivity, besides exerting a specific effect on hexokinase (glucosone) and UTP-trapping activity.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1573-4994
    Keywords: Na,K-ATPase ; fluorescent inhibitor ; kinetics ; energy transfer
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Abstract The interaction between the fluorescent ouabain derivative DEDO and purified renal Na,K-ATPase (isolated from different animal species) is investigated. Equilibrium binding studies provide a pK value of about 7.5 and a stoichoimetric coefficient of 1. Nonmodified ouabain exhibits the same affinity to the rabbit enzyme; the enzyme originating from the other sources binds DEDO 10 times less strongly than ouabain. Kinetic studies indicate that this is the consequence of a 10 times higher dissociation rate constant of the complexes formed with DEDO. The fluorescence emission intensity of DEDO is enhanced, being dependent on the enzyme source. The single decay time of DEDO is 3 ns in the absence and 21 ns in the presence of the rabbit enzyme and 14 ns in the presence of the pig renal enzyme. This result suggests that the fluorophore of DEDO is bound to a very hydrophobic environment of the enzyme. Further characterization of the static fluorescence spectra provides evidence for energy transfer between Trp residues of the enzyme and DEDO. Distance estimations suggest that one or two Trp residues are likely to be located in the proximity of the fluorophore.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Journal of fluorescence 6 (1996), S. 165-168 
    ISSN: 1573-4994
    Keywords: Cation binding ; fluorescence decay ; kinetics ; binding constants ; Na,K-ATPase ; eosin Y
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Abstract Time-resolved fluorescence and binding studies have been carried out on Na,K-ATPase in the presence of the fluorescent dye eosin Y to obtain thermodynamic and kinetic parameters for the interaction of the enzyme with different cations. Eosin Y binding is indicated by a 3 ns fluorescence decay process and is observed only in the presence of mono- and divalent cations. This type of cation binding is interpreted as a nonselective electrostatic interaction, with negatively charged groups of the enzyme providing a high-affinity eosin Y binding site. Eosin Y binding is observed only under conditions where the enzyme exists in the conformational state F1. The kinetic parameters of eosin Y binding have been determined employing stopped-flow fluorometry.
    Type of Medium: Electronic Resource
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