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  • 1990-1994  (1)
  • 1980-1984  (1)
  • 1975-1979
  • 5-fluorouracil  (1)
  • Lipocortin  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Colloid & polymer science 260 (1982), S. 511-513 
    ISSN: 1435-1536
    Keywords: 5-fluorouracil ; Sodium carboxymethylcellulose ; Interaction ; Enthalpy ; Viscosity
    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 interaction of an anticancer drug, 5-fluorouracil with sodium carboxymethylcellulose in aqueous solution was studied with a spectral method and viscosity measurement. From the binding data, the standard molar change in enthalpy, entropy and the number of binding sites on polymer were calculated. The standard molar change of enthalpy of 5-fluorouracil is about — 7 Kcal/mol with sodium carboxymethylcellulose. The enthalpy change is a considerably greater.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Archives of dermatological research 285 (1993), S. 296-299 
    ISSN: 1432-069X
    Keywords: Immunoblotting ; Immunohistochemistry ; Lipocortin ; Psoriasis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The distribution of lipocortin I, a steroid-induced inhibitory protein of phospholipase A2, was examined in normal and psoriatic human skin. Using immunoblotting analysis with specific antibody against human lipocortin I purified from human placenta, lipocortin I was detected as a 37 kDa protein in cultured epidermal cells, whole skin and epidermis. In the dermis and stratum corneum, lipocortin I was only weakly detectable by Western blotting. In contrast to normal skin, much less lipocortin I was detected by Western blotting analysis in psoriatic skin. Using immunoperoxidase immunohistochemical analysis, lipocortin I was demonstrated in the cytoplasm of keratinocytes in the upper and middle layers of the epidermis and in some infiltrating cells in the dermis in normal skin. In involved psoriatic skin, by contrast, lipocortin I was almost undetectable in the epidermis, although it was demonstrated in some infiltrating cells in the dermis. No immunostaining of lipocortin I was observed in the stratum corneum of normal or psoriatic skin. These results, together with the finding that phospholipase A2 activity is higher in psoriatic epidermis than in normal epidermis, suggest that lipocortin I plays an important role in the regulation of differentiation and proliferation of epidermal keratinocytes.
    Type of Medium: Electronic Resource
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