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  • Artikel: DFG Deutsche Nationallizenzen  (3)
  • Anacardiaceae  (1)
  • Arginase  (1)
  • GTP cyclohydrolase II  (1)
  • 1
    Digitale Medien
    Digitale Medien
    Amsterdam : Elsevier
    Phytochemistry 13 (1974), S. 1571-1574 
    ISSN: 0031-9422
    Schlagwort(e): 6,8''-naringeninylapigenin ; Anacardiaceae ; NMR data. ; Rhus succedanea ; flavanoflavone
    Quelle: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Thema: Biologie , Chemie und Pharmazie
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 2
    Digitale Medien
    Digitale Medien
    Springer
    Virchows Archiv 428 (1996), S. 325-331 
    ISSN: 1432-2307
    Schlagwort(e): Arginase ; Gastric cancer ; Immunohistochemistry
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Abstract High levels of arginase have been detected in gastric adenocarcinoma. To examine the hypothesis that this is due to macrophage infiltration into the tumour, we localized the cellular distribution of arginase by immunohistochemical staining. We examined gastric adenocarcinomas and their corresponding normal tissues (n=45), leiomyomas (n=2), leiomyosarcomas (n=3), human gastric adenocarcinoma cell lines (n=3), and benign gastric ulcers (n=4) by the avidin-biotin-peroxidase complex technique. Macrophages with strong arginase immunoreactivity were observed infiltrating both gastric normal and cancer tissues. No arginase immunoreactivity was observed in normal mucosal gland, muscular and serosal tissues or benign gastric ulcers. The immunoreactivity of arginase was positive but heterogeneous in most specimens of gastric adenocarcinoma (62.2%) and was absent from gastric intestinal metaplasia, leiomyomas and leiomyosarcomas. Among the 28 neoplasms with arginase immunoreactivity, scattered immunoreactivity was also noted in adjacent dysplastic glands in 12 (42.8%) specimens. Arginase immunoreactivity was observed in all three gastric cancer cell lines. Arginase is present in the cytoplasm but not in the nucleus. These data suggest that the high arginase levels in adenocarcinoma cancer tissues originate largely from cancer cells.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 3
    Digitale Medien
    Digitale Medien
    Springer
    Molecular genetics and genomics 261 (1999), S. 374-380 
    ISSN: 1617-4623
    Schlagwort(e): Key wordsEscherichia coli ; ribA ; GTP cyclohydrolase II ; SoxS binding ; RNA polymerase
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract The ribA gene, encoding GTP cyclohydrolase II in Escherichia coli, is a member of the soxRS regulon, which is induced by superoxide-generating agents. By evaluating lacZ expression driven by the ribA promoter carrying different lengths of upstream region in a monolysogen, we found that the superoxide-responsive element resides between 56 and 94 nucleotides upstream of the transcriptional start site. Purified SoxS protein bound to this region and protected nucleotides between positions −80 and −58 from degradation by DNase I. This region contains a putative SoxS-binding sequence (soxbox) in reverse orientation. The SoxS protein interacted specifically with four guanine residues within the soxbox sequence, as demonstrated by methylation interference analysis. These results clearly indicate that SoxS binds to the reversed soxbox sequence in the ribA gene, while in other known genes of the soxRS regulon it binds to the normally oriented soxbox. Possible modes of interaction between SoxS and RNA polymerase are discussed.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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