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  • 2005-2009
  • 1980-1984  (2)
  • 1960-1964
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  • 1900-1904
  • Cell-mediated immunity  (1)
  • Glycine  (1)
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Erscheinungszeitraum
  • 2005-2009
  • 1980-1984  (2)
  • 1960-1964
  • 1950-1954
  • 1905-1909
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  • 1
    Digitale Medien
    Digitale Medien
    Springer
    Journal of molecular medicine 60 (1982), S. 317-318 
    ISSN: 1432-1440
    Schlagwort(e): Adenosine deaminase ; Lymphocytes ; Cell-mediated immunity ; Hodgkin's disease ; Adenosine deaminase ; Lymphozyten ; Zellvermittelte Immunität ; Morbus Hodgkin
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Beschreibung / Inhaltsverzeichnis: Zusammenfassung Die Aktivität der Adenosindesaminase (EC3.5.4.4.) ADA in Blutplasma, Erythrozyten und Lymphozyten wurde bei 23 Patienten mit Morbus Hodgkin und teilweise bei 99 Referenzpersonen bestimmt. Die Enzymaktivitäten wurden mit Adenosin als Substrat und durch Analyse des Ammoniaks gemessen. Zwischen den ADA-Aktivitäten in Blutplasma, Erythrozyten und Lymphozyten wurde keine Korrelation festgestellt. Die Lymphozyten der Patienten wiesen niedrigere ADA-Aktivitäten auf als die Lymphozyten der Referenzpersonen. Die ADA-Aktivität in Plasma oder Erythrozyten ist nicht vermindert. Die herabgesetzten ADA-Aktivitäten in den Lymphozyten der Patienten können zur gestörten zellvermittelten Immunantwort bei Morbus Hodgkin in Beziehung gesetzt werden.
    Notizen: Summary The activity of adenosine deaminase (ADA) (EC3.5.4.4.) was determined in the blood plasma, erythrocytes, and lymphocytes of 23 patients with Hodgkin's disease and partly also in 99 control subjects. The enzyme activities were measured using adenosine as substrate and by analysis of ammonia. No correlation was found between the ADA activities in lymphocytes, erythrocytes, and blood plasma. The lymphocytes of the patients revealed lower ADA activities (U/g protein) than the lymphocytes of control subjects. The ADA activity is not reduced in plasma or erythrocytes. The lower activities of ADA in the lymphocytes of patients may be related to the impaired cell-mediated immunity of the Hodgkin's disease.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 2
    ISSN: 1432-072X
    Schlagwort(e): 5-Hydroxybenzimidazolylcobamide ; Vitamin B12-factor III ; Coenzyme F420 ; Methanosarcina barkeri ; Archaebacterium ; Corrin precursor ; C-5 pathway ; Glycine ; Glutamate ; Eubacteria
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract Exogenous 5-hydroxy-[2-14C]benzimidazole was transformed by Methanosarcina barkeri into 5-hydroxy-[2-14C]benzimidazolylcobamide. Thereby the endogenous biosynthesis of 5-hydroxybenzimidazole was completely blocked. Benzimidazole and 5,6-dimethylbenzimidazole were used by M. barkeri to form benzimidazolylcobamide respectively 5,6-dimethylbenzimidazolylcobamide (vitamin B12), but in these cases the endogenous biosynthesis of factor III was not completely suppressed. With [2-14C]benzimidazole it was demonstrated that this base as well as the benzimidazolylcobamide formed thereof are no precursors in the biosynthesis of 5-hydroxybenzimidazolylcobamide. Glycine instead was found to be a building block for the biosynthesis of 5-hydroxybenzimidazole, since radioactivity from [1-14C] and [2-14C]glycine was incorporated, into the base moiety of factor III, but not into its corrin moiety. With [1-13C]glycine and 13C-NMR-spectroscopy it was shown that C-1 of glycine gets C-3a of 5-hydroxybenzimidazole. [1-13C]glycine also led to a single prominent signal in the 13C-NMR-spectrum of coenzyme F420, this was assigned to C-10a. Thus C-1 of glycine was incorporated into the hydroxybenzene part of 5-hydroxybenzimidazole, whereas it was not incorporated into this part of coenzyme F420, indicating that the hydroxybenzene part of these two compounds is not formed from a common intermediate. L-[U-14C]glutamate led to the exclusive labeling of the corrin ring of factor III, showing that the corrin precursor 5-aminolevulinic acid is formed by the C-5 pathway in M. barkeri. These experiments indicate that the biosynthesis of factor III in the “archaebacterium” M. barkeri is similar to the corrinoid biosynthesis in the anaerobic “eubacteria” Eubacterium limosum, Clostridium barkeri, and Clostridium thermoaceticum.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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