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  • 1
    ISSN: 1432-1440
    Keywords: Thomsen-Friedenreich Antigen ; Erdnußagglutinin ; Neuraminidase ; Autoradiographie ; Fluorescenzmikroskop ie ; Thomsen-Friedenreich antigen ; Peanut agglutinin ; Neuraminidase ; Autoradiography ; Fluorescence microscopy
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Description / Table of Contents: Summary 1. Three different methods are described for the visualisation of the Thomsen-Friedenreich (TF) antigen on cell suspensions, formalin-fixed and paraffin embedded or frozen tissue sections: a) Rosette formation with chicken and sheep erythrocytes. b) Fluorescence-microscopy with fluorescein labelled peanut agglutinin. c) Autoradiography with3H-labelled peanut agglutinin. 2. The TF antigen was shown, as far as presently investigated, to be exposed on various blood cells, glomerula of the kidney and normal mammary gland after neuraminidase treatment. Mammary gland was also shown to possess TF receptors without prior treatment with neuraminidase. 3. The exposure of this cryptantigen can be brought about by bacterial or viral neuraminidase and is followed by an antigen/antibody reaction, which can lead to possible pathological consequences.
    Notes: Zusammenfassung 1. Drei verschiedene Methoden zur Darstellung von sog. Thomsen-Friedenreich (TF)-Antigenen in Zellsuspensionen, an Formalin-fixiertem und in Paraffin eingebettetem Gewebe sowie in Gefrierschnitten werden beschrieben: a) Rosetten-Bildung mit Hühner- und Schaferythrocyten. b) Fluorescenzmikroskopie mit Fluorescein-markiertem Erdnußagglutinin. c) Autoradiographie mit3H-markiertem Erdnußagglutinin. 2. Nach Neuraminidasebehandlung konnten TF-Antigene — soweit bisher untersucht — auf verschiedenen Blutzellen, in Nierenglomerula und in normalem Brustdrüsengewebe nachgewiesen werden. Ein Teil derartiger Antigene lag im Brustdrüsenparenchym auch bereits als freie Rezeptoren vor, d. h. waren nicht von Neuraminsäure bedeckt. 3. Die Freilegung dieser Kryptantigene kann im Rahmen von Infektionen durch bakterielle und virale Neuraminidase erfolgen. Dabei kommt es zu einer Antigen/Antikörper Reaktion mit unter Umständen klinisch relevanten Folgen.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-0843
    Keywords: Key words Dolastatin-10 ; Dolastatin-15 ; Liquid chromatography atmospheric pressure ; Mass spectrometry ; Phase I trial
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract A highly sensitive and specific assay for the quantitation of the anticancer agent dolastatin-10 (DOL-10) in human plasma is described. The method was based on the use of electrospray ionization-high-performance liquid chromatography/mass spectrometry (ESP-LC/MS). The analytical procedure involved extraction of plasma samples containing DOL-10 and the internal standard (DOL-15) with n-butyl chloride, which was then evaporated under nitrogen. The residue was dissolved in 50 μl mobile phase and 10 μl was subjected to ESP-LC/MS analysis using a C18 microbore column. A linear gradient using water/acetonitrile was used to keep the retention times of the analytes of interest under 5 min. The method exhibited a linear range from 0.005 to 50 ng/ml with a lower limit of quantitation (LLQ) at 0.005 ng/ml. Absolute recoveries of extracted samples in the 85–90% range were obtained. The method's accuracy (≤5% relative error) and precision (≤10% CV) were well within industry standards. The analytical procedure was applied to extract DOL-10 metabolites from samples obtained following incubation of the drug with an activated S9 rat liver preparation. Two metabolic products were detected and were tentatively identified as a N-demethyl-DOL-10 and hydroxy-DOL-10. Structural assignments were made based on the fragmentation patterns obtained using the electrospray source to produce collision-induced dissociation (CID). The method was also applied to the measurement of DOL-10 in the plasma of patients treated with this drug. Preliminary investigation of the pharmacokinetics suggested that drug distribution and elimination may be best described by a three-compartment model with t1/2α = 0.087 h, t1/2β = 0.69 h and t1/2γ = 8.0 h. Plasma clearance was 3.7 l/h per m2.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1432-1335
    Keywords: Thomsen-Friedenreich antigen ; Breast carcinoma ; Histochemistry ; Lectin ; Neuraminidase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Normal tissue as well as various benign and malignant lesions of the breast were histochemically examined for the presence of the Thomsen-Friedenreich (TF)-antigen. Fluorescein- or 3H-labelled peanut agglutinin was used for this purpose, a lectin that is known to have a high affinity for the TF-antigen. The occurrence of this TF-antigen seemed in all cases, even in the carcinoma lobulare in situ that is regarded as being derived from myoepithelial cells by some authors, to be associated with a secretory condition. Its presence (free and neuraminicacid covered) in normal, hyperplastic and malignant breast tissue, however, cannot be considered a specific tumour associated antigen as has been previously assumed. Furthermore the investigations have shown that the intensity of fluorescence for peanut agglutinin (PNA)-receptors was generally stronger in differentiated carcinomas than in undifferentiated carcinomas of the breast. The histochemical findings are discussed with regard to diagnostical and immunotherapeutical aspects.
    Type of Medium: Electronic Resource
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