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  • rat  (2)
  • Springer  (2)
  • American Institute of Physics
  • Copernicus
  • Public Library of Science
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  • Springer  (2)
  • American Institute of Physics
  • Copernicus
  • Public Library of Science
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  • 1
    Electronic Resource
    Electronic Resource
    Rat red blood cell hexokinase purification, properties and age-dependence (1986)
    Springer
    Molecular and cellular biochemistry 69 (1986), S. 179-185 
    Details
    ISSN: 1573-4919
    Keywords: hexokinase ; age-dependence ; red blood cells ; rat
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Summary Rat erythrocytes, in contrast to red blood cells from other mammals, have been shown to contain only one hexokinase isozymic form identified as type I by chromatographic and kinetic properties. Rat reticulocytes contain 3.6-times the hexokinase activity found in mature erythrocytes but exactly the same isozyme. By a combination of ion-exchange chromatography, dye-ligand chromatography and high-pressure liquid chromatography the rat erythrocyte hexokinase was purified more than 84 000-fold to a specific activity of 143 units/mg protein and shown to be homogeneous by sodium dodecyl sulfate-gel electrophoresis. The native protein showed a molecular weight of 100 000 by gel-filtration and an apparent molecular weight of 98 000 under denaturating conditions in sodium dodecyl sulfate-gel electrophoresis. The isoelectric point was shown to be 6.3 pH units. This data provides evidence of only one form of hexokinase in the erythrocytes of a mammal.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00224765
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  • 2
    Electronic Resource
    Electronic Resource
    Similarities and differences between human and rat hexokinases type I (1990)
    Springer
    Molecular and cellular biochemistry 94 (1990), S. 105-111 
    Details
    ISSN: 1573-4919
    Keywords: hexokinases I ; peptide mapping ; immunological properties ; human ; rat
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract The intracellular distribution and several properties of hexokinases type I purified to homogeneity from human placenta and rat brain were compared. The specific activity of the human enzyme was 190 ± 5 U/mg protein; 140 ± 5 U/mg protein that of the rat hexokinase. Comparative peptide mapping after limited tryptic digestion indicates a similar domain structure, however analogous experiments performed in the presence of substrates or effectors of the enzyme provide evidence of significant differences among hexokinases. Similarly, immunological studies with polyclonal and monoclonal antibodies while confirming some common epitopes also disclose important differences that cannot be expected on the basis of amino acid composition and of an in vivo identical function. These results are consistent with suggestions by several investigators that amino acid substitutions in mammalian hexokinases have occurred at a relatively fast rate during hexokinase type I evolution
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00214117
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