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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Archives of dermatological research 280 (1988), S. 380-384 
    ISSN: 1432-069X
    Keywords: Calpain ; Transglutaminase ; Thrombin ; Dimethyl sulfoxide ; Heating
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Two transglutaminases (TGase) with estimated molecular weight of 55,000 (55-K TGase) and 120,000 (120-K TGase) were partially purified from the cytosolic fraction of porcine skin (epidermis-rich preparation) using DEAE-cellulose and gel-filtration chromatographies. The enzyme activities of both trans-glutaminases were enhanced more than 20-fold by treatment with calpain (Ca2+-dependent cysteine proteinase) in the presence of Ca2+, and this enhancement was inhibited by adding EDTA, leupeptin, or an endogenous calpain-specific inhibitor protein (calpastatin). 55-K TGase was effectively activated by a smaller amount of calpain than was 120-K TGase, while known activating reagents such as thrombin and dimethyl sulfoxide or heat treatment preferentially activated 120-K TGase. One of the physiological functions of calpain in the epidermis may be the activation of epidermal transglutaminases.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Colloid & polymer science 261 (1983), S. 467-470 
    ISSN: 1435-1536
    Keywords: 5-trifluoromethyluracil ; Sodium poly-α,L-glutamate ; Interaction ; Viscosity ; 1-(2-tetrahydrofuryl)-5-fluorouracil
    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 to the correlations in term of chemical structure and the potentiactive drug activity. The interaction of 5-trifluoromethyluracil (although 5-trifluoromethyluracil do not used as anticancer drug, the structure of the compound has similar structure with 5-fluorouracil) 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 polymer were calculated. It is very interesting that the value ofδH
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Archives of dermatological research 282 (1990), S. 65-67 
    ISSN: 1432-069X
    Keywords: Transglutaminase ; Factor XIII ; Human epidermis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Colloid & polymer science 259 (1981), S. 350-353 
    ISSN: 1435-1536
    Keywords: Anticancer drug ; 1-(2-tetrahydrofuryl)-5-fluorouracil ; Sodium poly-α ; L-glutamate ; Interaction ; 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
    Description / Table of Contents: Zusammenfassung Die Wechselwirkung zwischen 1-(2-Tetrahydrofuryl)-5-fluorouracil und Na-Poly-α,L-glutamat wurde mit den Methoden der Spektroskopie und der Viskositätsmessung untersucht. Aus den Bindungsdaten wurden die molare Änderung von Entropie und Enthalpie und die Zahl der Brückenstellen des Polymeren berechnet. Der Wert von ΔG° beträgt ca. −10 Kcal/mol. Die Affinität ist also sehr groß.
    Notes: Summary The interaction of an anticancer drug, 1-(2-tetrahydrofuryl)-5-fluorouracil 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 polymer were calculated. The standard affinity of 1-(2-tetrahydrofuryl)-5-fluorouracil is about −10 kcal/ol with sodium poly-α,L-glutamate. The affinity is also very high.
    Type of Medium: Electronic Resource
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