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  • Protein content  (2)
  • degradation  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Adsorption of alachlor by montmorillonites (1997)
    Springer
    Journal of thermal analysis and calorimetry 50 (1997), S. 257-268 
    Details
    ISSN: 1572-8943
    Keywords: adsorption ; alachlor ; degradation ; montmorillonite
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The adsorption of the tertiary aromatic amide alachlor by Na-montmorillonite and Al-polyhydroxy-montmorillonite was investigated by DTA, XRD, SEM and Thermo-FTIR Spectroscopy. This molecule is adsorbed into the interlayer space of the montmorillonite, replacing interlayer water. In this organo-clay complex the interlayer water forms hydrogen bonds with N or O atoms of the tertiary amide group. Samples which were aged during six months degraded by hydrolysis to give mainly secondary amide. This reaction was catalysed by Al-polyhydroxy-montmorillonite more than by Na-montmorillonite.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01979566
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    The reserve proteins in the cells of mature cotyledons ofLupinus albus var.Lucky. I. Quantitative ultrastructural study of the protein bodies (1986)
    Springer
    Protoplasma 130 (1986), S. 120-127 
    Details
    ISSN: 1615-6102
    Keywords: Biometry ; Cotyledon ; Lupin ; Protein bodies ; Protein content
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary A quantitative ultrastructural study of the protein bodies of the lupin cotyledonary cells was performed to determine the protein content per cell. Two kinds of protein body were observed by transmission and scanning electron microscopy whatever the cellular type within the cotyledon. Some of these were conventional spherical structures, entirely filled with a dense protein matrix, others exhibited one large or several small light inclusions within the dense matrix. Even when a few light areas contained globoids, the majority remained of unknown nature, but could not be considered proteinaceous since they never reacted with specific protein dyes. The reserve protein content per cell was determined by image analysis on two seeds (L1 and L2) selected because they had a markedly different total protein content. The volume occupied by the dense matrix of the intracellular protein bodies was considered representative of the reserve protein quantity. The protein content per cell increased from the periphery to the centre of the cotyledon in the two seeds studied. The protein content per cell of the L2 seed was generally found to be greater than the L1 seed, in particular in the abaxial zone where it was markedly higher. The difference in total protein content of the two seeds was demonstrated to be primarily due to a differential alveolation of the protein bodies. These results will be used to study the relationship between the protein content of the cotyledonary cells and their nuclear DNA content.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01276593
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    The reserve proteins in the cells of mature cotyledons ofLupinus albus var.Lucky (1986)
    Springer
    Protoplasma 130 (1986), S. 128-137 
    Details
    ISSN: 1615-6102
    Keywords: Cotyledons ; DNA ; Endopolyploidy ; Lupin ; Protein content
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The nuclear DNA content of cotyledonary cells of two lupin seeds (L1 and L2) with markedly different total protein content, were investigated by scanning cytophotometry. Both seeds had polyloid nuclei with DNA levels varying between 8 C and 64 C, the majority being either 16 C or 32 C. The highest DNA levels were found in the abaxial and central cotyledonary zones of both seeds; seed L2 had a higher ploidy level than L1. It is shown that the volume of condensed chromatin (chromocenters) increased proportionally with the DNA content of the nucleus. A comparison was made between the distribution of protein, previously determined byLe Gal andRey (1986) and the DNA throughout the cotyledon. The L2 seed, which has the highest total protein and the highest protein content per cell, also exhibited the greatest DNA content per cell. For both seeds, the r-value for association of DNA and protein content per cell was highly significant (0.98).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01276594
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    Paper (German National Licenses)
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