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  • 1
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 223 (1969), S. 1064-1066 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The relative amounts of lysine-rich histone subfractions of the rabbit mammary gland show small but significant changes as the tissue progresses from pregnancy to lactation10. These observations were extended to pregnant and lactating rats, and Stellwagen11 noted that the ly sine-rich histone ...
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Molecular and cellular biochemistry 57 (1983), S. 81-92 
    ISSN: 1573-4919
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Summary The phosphorylation of H1 histones is reviewed. Consideration is given to phosphorylation reactions which occur in both replicating and nonreplicating cells. The available evidence suggests that H1 histones accept phosphate groups at different sites in response to different stimuli. The tentative location of the acceptor sites is summarized, and the effects of site-specific phosphorylation on the conformation of H1 histones in vitro is discussed. The phosphorylation of H1 histones which occurs during cell replication is reviewed in detail, and it is concluded that there is no clocklike mechanism which couples the phosphorylation of a particular site or region in H1 histones to a set point in the cell cycle. There is both species-and cell-specific variability in the phosphorylation of H1 histones during cell replication. Recent studies are discussed which show that an interspecific somatic cell hybrid of mouse and Chinese hamster can replicate the Chinese hamster genome in a stable manner using only mouse H1 histones and their phosphorylated forms. I speculate that H1 histone phosphorylation is a mechanism for the relaxation of long-term structures needed for differential gene activity in order to attain the short-term goal of genome replication.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Somatic cell and molecular genetics 6 (1980), S. 653-665 
    ISSN: 1572-9931
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract The synthesis of H1 histones was studied in nine mouse-human somatic cell hybrid clones containing reduced numbers of human chromosomes. The entire human genome could be accounted for karyologically and by the use of functional assays for specific enzyme markers encoded by human chromosomes. Chromatographic resolution and peptide mapping of species-specific H1 histones failed to reveal human H1 histones to a level of about 1% of total in the nine clones. In addition to the species-specific extinction of human H1 histones, effects were seen on the quantity of mouse H1 histone subtypes produced in four of the nine clones. The remaining five clones produced H1 histones qualitatively and quantitatively identical with those of the mouse parent, which was common to all nine clones. The results suggest at least two levels of control for H1 histone gene expression.
    Type of Medium: Electronic Resource
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