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  • 1980-1984  (2)
  • 1970-1974  (2)
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  • 1
    Electronic Resource
    Electronic Resource
    Detection of radiation from a heated and modulated equatorial electrojet current system (1984)
    [s.l.] : Nature Publishing Group
    Nature 311 (1984), S. 134-135 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The VHF heating experiments involved a research team from The Pennsylvania State University working in close cooperation with the Jicamarca Radar Observatory of the Geophysical Institute of Peru. Stubbe et al.1 successfully detected radiation from the polar electrojet above Tromso, Norway and ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/311134a0
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Variation of Electron Density in the D-region (1970)
    [s.l.] : Nature Publishing Group
    Nature 226 (1970), S. 1116-1117 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] THIS letter reports some tentative results of measurements of the D-region electron density made at the Pennsylvania State University during the solar eclipse of March 7, 1970, by the wave interaction technique described by Lee and Ferraro1. At Pennsylvania State University the eclipse was partial ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/2261116a0
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Fractionation of non-histone chromatin proteins from pig liver and kidney by means of immobilized histone H3 (1980)
    Springer
    Molecular and cellular biochemistry 30 (1980), S. 101-106 
    Details
    ISSN: 1573-4919
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Summary The non-histone chromatin proteins (NHCp) from pig liver and kidney have been partially fractionated in non-denaturing conditions by the use of histone H3 immobilized on agarose and the fractions obtained have been analysed by SDS-polyacrylamide gel electrophoresis and amino acid analysis. At least six different fractions have been obtained by successive increases of the ionic strength of the medium. Few NHCp have been evidentiated with subunit molecular weights 55,000 and less than 30,000, which display a remarkably high affinity for histone H3, and require 5 M urea to be displaced from the immobilized histone. The elution patterns of the NHCp from liver and kidney, although very similar, reveal some significant differences between the two tissues, which are undetectable by SDS-electrophoresis and which are most likely due to tissue specific proteins. This histone-affinity chromatography appears to be a promising approach for the analysis of specific histone-NHCp interactions, and as a first step for NHCp purification.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00227924
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Far-infrared spectra of some globular proteins (1971)
    New York : Wiley-Blackwell
    Biopolymers 10 (1971), S. 2377-2386 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The far-infrared absorption spectrum (40-400 cm-1) of solid pellets and films of several globular proteins (lysozyme, myoglobin, hemoglobin, serum albumin, ribonuclease, chymotrypsinogen, subtilisin) and of some representative polypeptides [nylon 66, poly (γ-benzyl L-glutamate)] have been investigated by using a Michelson interferometer. While polypeptides are known to present several peaks which can be assigned mostly to hydrogen-bond modes, all the investigated globular proteins display only one broad, intense baud in the 100-200 cm-1 region. The origin of this band, which persists even after denaturation or partial digestion, is discussed.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.360101203
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    Paper (German National Licenses)
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