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  • Nitrogen storage  (2)
  • gelatin  (2)
  • Springer  (4)
  • American Chemical Society
  • American Institute of Physics
  • Copernicus
  • PANGAEA
  • Springer Nature
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  • Springer  (4)
  • American Chemical Society
  • American Institute of Physics
  • Copernicus
  • PANGAEA
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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Trees 5 (1991), S. 153-157 
    ISSN: 1432-2285
    Keywords: Bark proteins ; Nitrogen storage ; Hardwoods ; Overwintering
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Summary Bark proteins of eight temperate hardwoods were analyzed by SDS-PAGE at monthly intervals to determine whether an accumulation of specific proteins, potential storage proteins, occurred in the fall at the time of leaf senescence. Storage proteins were identified as proteins that accumulated during the fall and were present in reduced amounts in the summer. Total protein levels were higher in the winter than in the summer in Fagus sylvatica, Fraxinus americana, Tilia americana, Alnus glulinosa, Betula papyrifera and Querus rubra, but not in Gleditsia triacanthos or Robinia pseudoacacia. Betula contained the most abundant storage protein, although in all species minor bands, which fluctuated seasonally, could be identified. With the exception of Alnus and Betula, results generally correlated with previous microscopy studies of these tree species, which showed varying amounts of protein storage vacuoles present in phloem parenchyma cells during the winter, but not during the summer.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Trees 5 (1991), S. 196-202 
    ISSN: 1432-2285
    Keywords: Protein-storage vacuole ; Protein body ; Softwoods ; Nitrogen storage ; Overwintering
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Summary The seasonal occurrence of protein-storage vacuoles in parenchyma cells of the inner bark and leaf tissues of seven softwood species was examined. Previously published results showed that these organelles often fill the phloem parenchyma cells of the inner bark tissues in overwintering hardwoods, whereas they are absent from this tissue during the summer. We hypothesize that the organelles are involved in the storage of reduced nitrogen during wintering, in a manner analogous to protein bodies of seeds. A survey of the phloem and cambial parenchyma tissues in six evergreen softwood species (Pinus strobus, P. sylvestris, Picea abies, P. glauca, Abies balsamea, and Thuja occidentalis) and in one deciduous softwood species (Larix decidua) was conducted. There was a large variation in the degree and timing of protein-storage vacuole formation between the individual genera and species. The organelles were not seen in summer samples of inner bark tissues of any of the genera or species examined. Protein-storage vacuoles were common in the bark tissues of Pinus, Abies and Thuja, occasionally seen in Picea, and rarely found in Larix during the winter. One-year-old leaves were also examined, since in all but Larix they are overwintering structures and can act as potential sites of nitrogen storage. Protein-storage vacuoles were present in Pinus and Thuja leaf tissue in both summer and winter, in Abies during winter only, and were absent from Picea leaf tissue at all times. These results indicate that the formation of protein-storage vacuoles prior to overwintering is not a ubiquitous phenomenon in softwoods.
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  • 3
    ISSN: 1435-1536
    Keywords: Circular dichroism ; gelatin ; sodium alkyl sulphates ; aqueousgelatinsolutions ; secondary structure ; pH ; temperature
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
    Notes: Abstract The modification of the triple helical structure in aqueous gelatin solutions by changing pH and adding alkyl sulphates at 298 K and after rechilling the solution to 283 K was investigated by CD-measurement. At 298 K the triple helical content at the IEP of the gelatin has its maximum value. It is only weakly affected by adding sodium dodecyl sulphate (SDDS) at concentrations 〈10−4 M/dm3. The unfolding of the triple helix affected by pH and SDDS is reversible by rechilling the solution. The triple helical content of gelatin solutions decreases at SDDS concentrations higher than 10−4 M/dm3. In all cases the decrease of the amount of triple helical structure is connected with an increase of the cis-configuration in single chains and leads to chain reversals. At sufficiently high SDDS concentrationsβ-sheets are formed. These changes are thermally irreversible. Sodium decyl sulphate (SDS) has a more minor influence than SDDS except in the range of the c.m.c. of SDS. At sufficiently high SDS concentrations,β-turns appear.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1435-1536
    Keywords: Circulardichroism ; gelatin ; nonionicsurfactants
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
    Notes: Abstract Using CD-measurements the influence of nonionic surfactants (dodecyl polyoxyethylene, ethoxylated para tert. octyl phenol, commercial nonionic WON 100 and octyl diethyl phosphinoxid) on the secondary structure of gelatin in aqueous solutions was investigated. At surfactant concentrations smaller than the c.m.c. the triple helical content of the gelatin is increased. At concentrations exceeding the c.m.c. the triple helical content decreases. Chain reversals of the peptide chains after the destruction of the triple helical structure were shown to appear in acidic environment at 298 K. This destruction is reversible by rechilling the solution.
    Type of Medium: Electronic Resource
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