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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Molecular biology reports 10 (1985), S. 153-158 
    ISSN: 1573-4978
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Complexes of histone H1 from sea urchin sperm (H1S) and calf thymus (H1T) with superhelical DNA I and relaxed circular DNA II have been analyzed by analytical sedimentation. Similar to H1T, the highly basic and relatively arginine-rich histone H1S preferentially interacts with DNA I compared to DNA II under competition conditions. However, H1S induces a stronger aggregation of bothforms of DNA than H1T. Below 0.05 M NaCl, the soluble complexes formed by both histones have similar properties, but aggregation proceeds in a different manner: H1S induces a stronger aggregation of DNA II as compared to DNA I, whereas H1T fails to aggregate DNA I. The results are explained on the basis of differences in amino acid sequence and structure of the two histones and related to the special chromatin condensing ability of histone H1S.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1573-4978
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A comparative study of the condensation of reconstituted complexes of circular SV40 DNA with core histones from calf thymus and sea urchin sperm was performed using sedimentation and electron microscopic techniques. It is shown that in low ionic strength solutions both types of complexes are similar to native ‘minichromosomes’. In the region from 0.08 to 0.16 M NaCl the complexes of SV40 DNA with thymus histones form small compact particles. By contrast, the compaction of the SV40 DNA complexes with sperm histones results in the formation of giant intermolecular associates. The results obtained may mean that histone H2B of sea urchin sperm participates in the formation of a higher order structure in sperm chromatin.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    New York : Wiley-Blackwell
    Biopolymers 13 (1974), S. 2077-2085 
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The sedimentation behaviour of DNP samples from calf thymus partially depleted of protein was studied. Upon transition from DNP to DNA a twofold decrease of the sedimentation constant, S02 0,W was observed. The translational friction coefficient f of DNP calculated from S02 0,W does not change at deproteinization, whereas the intrinsic viscosity [η] increases notably. Such difference in the dependence of f and [η] on the protein content is interpreted in terms of the theories for semirigid coils. The application of different models of DNP structure for the description of the hydrodynamic behaviour of DNP is considered. A model of the semirigid coil formed by a DNP chain partly folded into the superhelix seems to be most preferable.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
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