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  • 1990-1994  (2)
  • 1985-1989  (3)
  • Tumor promotion  (2)
  • 5-trifluoromethyluracil  (1)
  • Aging  (1)
  • Degradation products
  • [abr] CPB; beads of curdlan type polysaccharide 13140, β-1,3-glucan
Source
Material
Years
Year
Keywords
  • 1
    Electronic Resource
    Electronic Resource
    Interaction of 5-fluorouracil with sodium poly-α,L-glutamate (1985)
    Springer
    Colloid & polymer science 263 (1985), S. 682-685 
    Details
    ISSN: 1435-1536
    Keywords: 5-trifluorouracial ; sodium poly-α ; L-glutamate ; interaction ; viscosity ; 5-trifluoromethyluracil
    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 purpose of our research is to obtain an understanding of the binding mechanism and its correlations in terms of chemical structure and the potentiactive drug activity. The interaction of 5-fluorouracil (5-fluorouracil is used as an anticancer drug) with sodium poly-α,L-glutamate in aqueous solution was studied with a spectral method and viscosity measurement. From the binding data, the molar change in enthalpy, entropy and the number of binding sites on the polymer were calculated. It is very interesting that the value ofΔH0 of the binding of 5-fluorouracil with sodium poly-α,L-glutamate is smaller than that of 5-trifluoromethyluracil (although 5-trifluoromethyluracil is not used as an anticancer drug, the compound has a similar structure to 5-fluorouracil).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01419893
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Increased expression of the ornithine decarboxylase gene in mouse skin by ultraviolet light: detection by in situ hybridization technique (1990)
    Springer
    Archives of dermatological research 282 (1990), S. 487-489 
    Details
    ISSN: 1432-069X
    Keywords: Ornithine decarboxylase ; Gene expression ; Ultraviolet light ; Tumor promotion ; In situ hybridization
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00402630
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    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Increase in the expression of the ornithine decarboxylase gene in mouse skin by ultraviolet light (1989)
    Springer
    Archives of dermatological research 281 (1989), S. 514-516 
    Details
    ISSN: 1432-069X
    Keywords: Ornithine decarboxylase ; Gene expression ; Ultraviolet-B ; Tumor promotion ; Photocarcinogenesis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00510092
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Density-associated changes in platelet-activating factor acetylhydrolase activity and membrane fluidity of human erythrocytes (1994)
    Springer
    Annals of hematology 69 (1994), S. 139-145 
    Details
    ISSN: 1432-0584
    Keywords: Aging ; Erythrocytes ; Platelet-activating factor ; Acyltransferases ; Membrane fluidity
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Platelet-activating factor acetylhydrolase is known to degrade oxidatively fragmented phospholipids which are similar in structure to platelet-activating factor. We examined changes of acetylhydrolase activity during in vivo aging of human erythrocytes and tried to assess its role in maintaining the membrane properties of erythrocytes. Higher-density erythrocytes are enriched with older cells. Erythrocytes obtained from seven healthy colleagues were separated into four density fractions by centrifugation in discontinuous Percoll density gradients. Both membrane and cytosolic acetylhydrolase decreased with increasing erythrocyte density. Membrane and cytosolic acetylhydrolase activities in the lightest fraction were 2.0±1.0 (SD) nkat/g protein and 362±58 pkat/g protein, respectivley, and these values were significantly higher than those in the densest fraction: 1.3±0.7 nkat/g protein and 286±70 pkat/g protein, respectively. Membrane acyltransferase activity also decreased with red cell density and the average values in the lightest and densest fractions were 51.2±23.6 and 27.0±20.2 μkat/g protein, respectively. Generation of thiobarbituric acid-reactive substances induced byt-butyl hydroperoxide treatment decreased with increasing cell density, and the inhibition of acetylhydrolase with diisopropylfluorophosphate resulted in enhanced peroxide-induced lipid oxidation, particularly in lower-density fractions. There was no significant change in basal levels of thiobarbituric acid-reactive substances in red cell membrane. Membrane fluidity was evaluated by fluorescence recovery after photobleaching and it decreased as erythrocyte density increased. We conclude that the activity of the deacylation/reacylation cycle maintained by acetylhydrolase and acyltransferase is gradually reduced during in vivo aging of erythrocytes. This may be connected with decreases of polyunsaturated fatty acids and membrane fluidity in old eryhtrocytes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01695695
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    Paper (German National Licenses)
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  • 5
    Electronic Resource
    Electronic Resource
    HPLC analysis of human epidermal growth factor using immunoaffinity precolumn. II. Determination of hEGFs in biological fluids (1989)
    Springer
    Chromatographia 27 (1989), S. 574-580 
    Details
    ISSN: 1612-1112
    Keywords: Immunoaffinity chromatography ; Human epidermal growth factor (hEGF) ; Degradation products ; Immunoaffinity precolumn ; HPLC column-switching system
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary A high-performance liquid-chromatographic, column-switching system for automated sample pre-treatment and determination of human epidermal growth factor and its degradation products (hEGFs) is described. The system consists of an immunoaffinity precolumn (4.0×10mm) packed with diol silica immobilized with antibody against hEGF and an analytical ODS column (4.6×250mm). Samples such as cultured media ofE. coli, human urine, milk, seminal fluid and saliva can be directly injected on the immunoaffinity precolumn and the analytes of interest are trapped by the immobilized anti-hEGF antibody. After washing this precolumn with aqueous solvents, the analytes are desorbed with an aqueous solution of low pH and transferred to the analytical column to allow their separation in reversed phase mode. The recoveries of hEGFs spiked in these biological fluids were over 98%. The detection limit was 1 ng for a 1ml sample injection. This method was applied for the determination of hEGF levels in cultured media ofE. coli and biological fluids. Degradation of hEGF in human serum and urine was also examined.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02258981
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    Paper (German National Licenses)
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