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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    International journal of legal medicine 86 (1981), S. 221-225 
    ISSN: 1437-1596
    Keywords: 4-Hydroxycoumarin, identification ; Derivative spectroscopy, coumarin ; Cumarinderivate, Nachweis ; Derivativspektroskopie, Cumarin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine , Law
    Description / Table of Contents: Zusammenfassung Vorgestellt wird eine schnelle Nachweismethode für 4-Hydroxicumarine aus Organen oder Blutproben. Bei Verwendung eines Ultraschallhomogenisators ist die Analyse nach spätestens 30 min abgeschlossen. Die Identifizierung der Cumarinderivate erfolgt durch Derivativ-UV-Spektroskopie im Normalspektrum und dessen 1. Ableitung bei 340–240 nm. Als weiteres Nachweisverfahren kann zusätzlich die HPTLC angewendet werden.
    Notes: Summary Presented here is a rapid method of identifying 4-hydroxycoumarins in organs or blood samples. Using an ultrasonic homogenizer, a complete analysis is obtained in less than 30 min. Coumarin derivatives are identified by means of derivative UV spectroscopy in the normal spectrum and its first derivation at 340 to 240 nm. HPTLC can be employed as supplementary identification method.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1573-4919
    Keywords: brefeldin A ; ADP-ribosylation ; Golgi complex ; G proteins ; membrane transport ; inhibitors of ADP-ribosylation reaction
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract The fungal toxin brefeldin A (BFA) dissociates coat proteins from Golgi membranes, causes the rapid disassembly of the Golgi complex and potently stimulates the ADP-ribosylation of two cytosolic proteins of 38 and 50 kDa. These proteins have been identified as the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and a novel guanine nucleotide binding protein (BARS-50), respectively. The role of ADP-ribosylation in mediating the effects of BFA on the structure and function of the Golgi complex was analyzed by several approaches including the use of selective pharmacological blockers of the reaction and the use of ADP-ribosylated cytosol and/or enriched preparations of the BFA-induced ADP-ribosylation substrates, GAPDH and BARS-50. A series of blockers of the BFA-dependent ADP-ribosylation reaction identified in our laboratory inhibited the effects of BFA on Golgi morphology and, with similar potency, the ADP-ribosylation of BARS-50 and GAPDH. In permeabilized RBL cells, the BFA-dependent disassembly of the Golgi complex required NAD+ and cytosol. Cytosol that had been previously ADP-ribosylated (namely, it contained ADP-ribosylated GAPDH and BARS-50), was instead sufficient to sustain the Golgi disassembly induced by BFA. Taken together, these results indicate that an ADP-ribosylation reaction is part of the mechanism of action of BFA and it might intervene in the control of the structure and function of the Golgi complex.
    Type of Medium: Electronic Resource
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