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  • 1
    Electronic Resource
    Electronic Resource
    Metabolic denitrosation of diphenylnitrosamine: a possible bioactivation pathway (1987)
    Springer
    Journal of cancer research and clinical oncology 113 (1987), S. 131-136 
    Details
    ISSN: 1432-1335
    Keywords: N-Nitrosamines ; Metabolism ; Denitrosation ; Activation ; Inactivation ; Single strand breaks ; Hepatocytes ; Chinese hamster V 79 cells
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Nitrosodiphenylamine was tested for induction of DNA single strand breaks in rat hepatocytes and Chinese hamster V 79 cells with the alkaline filter elution assay. While in rat hepatocytes DNA damage was observed, negative results were obtained in V 79 cells. In view of the metabolic capacity of hepatocytes and the chemical structure of nitrosodiphenylamine it seems likely that cytochrome P-450-dependent, reductive denitrosation might be necessary for exerting this effect. Therefore the metabolism of nitrosodiphenylamine was investigated in phenobarbital-induced mouse liver microsomes and some of the metabolites were also tested. One metabolite was identified as diphenylamine whereas the others were identified as a ring-hydroxylated derivative of diphenylamine and its corresponding quinoneimine. Diphenylhydroxylamine which was not detected in the microsomes as a metabolite produced a significant amount of DNA single strand breaks in V 79 cells. When diphenylhydroxylamine was incubated with microsomes electron spin resonance spectrum was observed which indicated the formation of the diphenylnitroxide radical. This radical seems to be mediated by auto-oxidation rather than by enzymatic catalysis. Whether diphenylhydroxylamine might be responsible for the observed genetoxic effects of nitrosodiphenylamine assumed to be produced via active oxygen species is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00391434
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Toward an understanding of the fluorescence intensity changes observed on fluorescein 5′-Isothiocyanate-Na+,K+-ATPase (1994)
    Springer
    Journal of fluorescence 4 (1994), S. 251-254 
    Details
    ISSN: 1573-4994
    Keywords: Fluorescence spectra ; fluorescence decay ; dissociation constants ; fluorescein 5′-isothiocyanate ; FITC-fluorescein 5′-isothiocyanate-Na+,K+-ATPase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Abstract The fluorescence emission intensity between the Na+, and the K+ complex of Na+,K+-ATPase, labeled with fluorescein 5′-isothiocyanate (FITC), differs by 30 to 40%. Experimental studies are carried out to elucidate the physical reasons which account this intensity difference. The dissociation constant of protolysis of the covalently bound FITC and its fluorescence decay times are determined in media of different ionic compositions and are compared with the corresponding properties of a synthetic model compound. The fluorophore bound to the protein is characterized by two decay times in the nanosecond range; the model compound, by a single one. The static fluorescence intensity changes are discussed on the basis of these results.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01878459
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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