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  • 1
    Electronic Resource
    Electronic Resource
    Atmospheric transport of pollutants from North America to the North Atlantic Ocean (1984)
    [s.l.] : Nature Publishing Group
    Nature 308 (1984), S. 722-724 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Documenting source-transport-receptor relationships to pollution studies is an elusive, complex problem which contributes to most of the controversy over the origin of acid deposition in non-urban areas. While the combination of ground-based chemical measurements, meteorological trajectory analyses ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/308722a0
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Geology: So you thought mountain ranges were complicated (1984)
    [s.l.] : Nature Publishing Group
    Nature 312 (1984), S. 600-600 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] REMEMBER the time when it was thought that the major features of the Earth's crust were riveted in place as securely as armour plates on a battleship? It took courage to be a tectonic theorist, but life may have been easier for the quadrangle-mapper. In those days, crustal blocks mostly moved up ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/312600a0
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  • 3
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    Coenzyme function of cobalamin analogues from calf kidney (1984)
    American Society of Hematology
    Details
    Publication Date: 1984-07-01
    Description: Calf kidney has been used as a tissue source for the isolation of cobalamin analogues, which are defined here as cobalt-containing compounds of distinctive chromatographic behavior that are extractable from tissues by methods conventionally used to extract cobalamin and which, in radioisotope dilution assays, are more active with R-protein as binder than intrinsic factor and are relatively less active in microbiologic assays. Preparatory methods employed reverse affinity chromatography or a series of chemical extractions for the isolation of corrin followed by Dowex-50 chromatography. An analogue-containing fraction (peak 2) was eluted by acetate buffers between pH 4 and 5. This material was shown to contain cobalt, to migrate differently than the four cobalamins in Dowex-50 and paper chromatography, and to display a pattern of properties that is compatible with the above definition of cobalamin analogues. These analogues stimulated crude preparations of N5-methyltetrahydrofolate-homocysteine methyltransferase (EC 2.1.1.13) from Escherichia coli and rat liver at far lower concentrations (1–40 nmol/L) than the major cobalamins. No evidence of enzymatic conversion of cobalamin to analogue could be demonstrated.
    Print ISSN: 0006-4971
    Electronic ISSN: 1528-0020
    Topics: Biology , Medicine
    Published by American Society of Hematology
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  • 4
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    Coenzyme function of cobalamin analogues from calf kidney (1984)
    American Society of Hematology
    Details
    Publication Date: 1984-07-01
    Description: Calf kidney has been used as a tissue source for the isolation of cobalamin analogues, which are defined here as cobalt-containing compounds of distinctive chromatographic behavior that are extractable from tissues by methods conventionally used to extract cobalamin and which, in radioisotope dilution assays, are more active with R-protein as binder than intrinsic factor and are relatively less active in microbiologic assays. Preparatory methods employed reverse affinity chromatography or a series of chemical extractions for the isolation of corrin followed by Dowex-50 chromatography. An analogue-containing fraction (peak 2) was eluted by acetate buffers between pH 4 and 5. This material was shown to contain cobalt, to migrate differently than the four cobalamins in Dowex-50 and paper chromatography, and to display a pattern of properties that is compatible with the above definition of cobalamin analogues. These analogues stimulated crude preparations of N5-methyltetrahydrofolate-homocysteine methyltransferase (EC 2.1.1.13) from Escherichia coli and rat liver at far lower concentrations (1–40 nmol/L) than the major cobalamins. No evidence of enzymatic conversion of cobalamin to analogue could be demonstrated.
    Print ISSN: 0006-4971
    Electronic ISSN: 1528-0020
    Topics: Biology , Medicine
    Published by American Society of Hematology
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
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