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  • rat  (2)
  • Cavitation  (1)
  • Springer  (3)
  • American Institute of Physics
  • Copernicus
  • Public Library of Science
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  • Springer  (3)
  • American Institute of Physics
  • Copernicus
  • Public Library of Science
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  • 1
    ISSN: 0931-1890
    Keywords: Key words Aleppo pine ; Climate change ; Water stress ; Cavitation ; Transpiration
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Abstract  The present study was carried out to elucidate the response mechanisms of 50-year-old Pinus halepensis Mill. trees to a long-term and severe drought. The amount of water available to trees was artificially restricted for 12 months by covering the soil with a plastic roof. Over the short term a direct and rapid impact of drought was evident on the water relations and gas exchanges of trees: as the soil dried out in the Spring, there was a concurrent decrease of predawn water potential; transpiration was strongly reduced by stomatal closure. Seasonal changes in the water volume fractions of twig and stem xylem were observed and interpreted as the result of cavitation and refilling in the xylem. When droughted trees recovered to a more favourable water status, refilling of embolized xylem was observed; twig predawn water potentials were still negative in the period when the embolism was reversed in the twig xylem. A few months after the removal of the covering, no differences in whole plant hydraulic resistance were observed between droughted and control trees. Needle and shoot elongation and stem radial growth were considerably reduced in droughted trees; no strategy of trees to allocate carbon preferentially to the stem conducting tissues was apparent throughout the experiment. An after-effect of the drought on growth was observed.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Molecular and cellular biochemistry 69 (1986), S. 179-185 
    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
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Molecular and cellular biochemistry 94 (1990), S. 105-111 
    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
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