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  • 1970-1974  (2)
  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 23 (1974), S. 0 
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract— 〈list xml:id="l1" style="custom"〉1Chromatin protein fractions were separated from the nuclei from brain, liver and kidney of the guinea pig. The fractions were studied by electrophoretic methods and amino acid analysis.2Brain nuclear fractions were washed with 0.15m-NaCl and nuclear acidic proteins then removed by 0.35 m-NaCl. These 0.35 m-NaCl-extracted proteins were considered to be similar to the nuclear soluble acidic proteins.3Nonhistone-1, histone and nonhistone-2 fractions were obtained from 2.0 m-NaCl-soluble chromatin fractions by lowering the salt concentration and successive extraction with acid and alkali. The nonhistone-3 fraction was also extracted from the nuclear residue by alkaline solution.4The contents and characteristics of the nonhistone fractions of the brain, especially the nonhistone-1 fraction, differed among the three tissues. The histone fractions showed no obvious difference among the three tissues. The nonhistone-1 fraction of the brain, which comprised a low percentage of total nuclear protein, contained relatively high amounts of acidic proteins.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Origins of life and evolution of the biospheres 4 (1973), S. 490-504 
    ISSN: 1573-0875
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Geosciences
    Notes: Abstract The reactivity of cytochromesc derived from various organisms withPseudomonas aeruginosa nitrite reductase and cow cytochrome oxidase has been studied. Generally, cytochromesc isolated from primitive organisms react very rapidly with the bacterial nitrite reductase but do not react with cow cytochrome oxidase while those from higher organisms react poorly with the nitrite reductase but react very rapidly with the animal oxidase. The reactivity of cytochromec with the bacterial nitrite reductase reflects very well the evolutionary position of the organism from which it is isolated, while that with cow cytochrome oxidase seems to be related to the extent of adaptation of the parent organism to molecular oxygen. The results obtained in the present investigation suggests that cytochromec molecule which reacts very rapidly with the bacterial nitrite reductase but does not react with cow cytochrome oxidase has evolved to that which reacts very poorly with the nitrite reductuase but reacts very rapidly with the animal oxidase. It is also inferred that the evolution of cytochromec molecule may be caused by the evolution of cytochrome oxidase, and that the latter may be intimately related to genesis of molecular oxygen in the biosphere.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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