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  • 1
    Online Resource
    Online Resource
    Verwertungsstudie zur Erprobung und Einführung von point-of-care Diagnostik in China : Abschlussbericht ; China-PoCT ; Laufzeit: 1. Oktober 2006 - 31. August 2007 (2007)
    München : Fraunhofer Inst. für Zuverlässigkeit und Mikrointegration (IZM)
    Details Availability
    Keywords: Forschungsbericht ; China ; Gesundheitswesen ; Diagnostik ; Mikrosystemtechnik ; Mikrosensor ; Chip
    Type of Medium: Online Resource
    Pages: Online-Ressource (204 S., 3,12 MB) , Ill., graph. Darst., Kt.
    URL: https://edocs.tib.eu/files/e01fb08/588460710.pdf
    URL: https://doi.org/10.2314/GBV:588460710
    URL: https://edocs.tib.eu/files/e01fb08/588460710l.pdf
    DOI: 10.2314/GBV:588460710
    Language: German , Chinese , English
    Note: Förderkennzeichen BMBF 16SV3511. - Text teilw. in dt., engl. u. chin. Sprache , Unterschiede zwischen dem gedruckten Dokument und der elektronischen Ressource können nicht ausgeschlossen werden , Auch als gedr. Ausg. vorhanden , Systemvoraussetzungen: Acrobat reader.
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  • 2
    Electronic Resource
    Electronic Resource
    Xanthine dehydrogenase from the phototrophic purple bacterium Rhodobacter capsulatus is more similar to its eukaryotic counterparts than to prokaryotic molybdenum enzymes (1998)
    Oxford BSL : Blackwell Science Ltd, UK
    Molecular microbiology 27 (1998), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Fourteen Rhodobacter capsulatus mutants unable to grow with xanthine as sole nitrogen source were isolated by random Tn5 mutagenesis. Five of these Tn5 insertions were mapped within two adjacent chromosomal EcoRI fragments hybridizing to oligonucleotides synthesized according to conserved amino acid sequences of eukaryotic xanthine dehydrogenases. DNA sequence analysis of this region revealed two open reading frames, designated xdhA and xdhB, encoding xanthine dehydrogenase. The deduced amino acid sequence of XDHA contains binding sites for two [2Fe–2S] clusters and FAD, whereas XDHB is predicted to contain the molybdopterin cofactor. In contrast to R. capsulatus, these three cofactor binding sites reside within a single polypeptide chain in eukaryotic xanthine dehydrogenases. The amino acid sequence of xanthine dehydrogenase from R. capsulatus showed a higher degree of similarity to eukaryotic xanthine dehydrogenases than to the xanthine dehydrogenase-related aldehyde oxidoreductase from Desulphovibrio gigas. The expression of an xdhA–lacZ fusion was induced when hypoxanthine or xanthine was added as sole nitrogen source. Mutations in nifR1 (ntrC) and nifR4 (rpoN, encoding σ54) had no influence on xdh gene expression. A putative activator sensing the availability of substrate seems to respond to xanthine but not to hypoxanthine. The transcriptional start site of xdhA was mapped by primer extension analysis. Comparison with known promoter elements revealed no significant homology. Xanthine dehydrogenase from R. capsulatus was purified to homogeneity. The enzyme consists of two subunits with molecular masses of 85 kDa and 50 kDa respectively. N-terminal amino acid sequencing of both subunits confirmed the predicted start codons. The molecular mass of the native enzyme was determined to be 275 kDa, indicating an α2β2-subunit structure. Analysis of the molybdenum cofactor of xanthine dehydrogenase from R. capsulatus revealed that it contains the molybdopterin cofactor and not a molybdopterin dinucleotide derivative.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2958.1998.00733.x
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  • 3
    Electronic Resource
    Electronic Resource
    Reinvestigation of regulation of biosynthesis and subunit composition of nickel-dependent Hup-hydrogenase of Rhodospirillum rubrum (1992)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 91 (1992), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Regulation of biosynthesis and structural properties of the membrane-bound ‘hydrogen uptake’ (Hup)-hydrogenase of Rhodospirillum rubrum were studied. Under photoheterotrophic conditions, the highest activities were recorded in media with l-lactate, the lowest activities with malate. At high concentrations (20–40 mM), NH4+ or glutamate suppressed biosynthesis of hydrogenase. In culture media supplemented with 0.5 mM EDTA, normal Hup activities were only obtained in the presence of high concentrations of Ni2+ (80–150 μM). Activation of hydrogenase biosynthesis by Ni2+ was completely inhibited by chloramphenicol. The enzyme, solubilized from intracytoplasmic membranes by Triton X-114 and partially purified by gelfiltration, had a Mr of about 100 000. When analysed by SDS-PAGE, the native enzyme yielded three different protein bands with Mr values of 40 000, 34 000 and 29 000.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1992.tb05208.x
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  • 4
    Electronic Resource
    Electronic Resource
    EDTA activation of H2 photoproduction by Rhodospirillum rubrum (1992)
    Springer
    Applied microbiology and biotechnology 37 (1992), S. 496-500 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary The effect of trace elements (Fe, Ni) and chelating compounds on the activity of hydrogen (H2) uptake (Hup) hydrogenase, nitrogenase and rate and yield of H2 photoproduction from l-lactate in photosynthetic cultures of Rhodospirillum rubrum was investigated. Hup activity depended on the availability of Ni2+ and was inhibited by EDTA (0.3–0.5 mm ethylenedinitrilotetraacetic acid). Addition of EDTA (0.5 mm) to the culture medium caused a nearly complete inactivation of Hup activity and activation of nitrogenase, which was paralleled by a threefold increase in total H2 photoproduced from lactate. Hup− mutants, isolated by transposon Tn5 mutagenesis, produced maximally twofold more H2 than the wild-type. Experiments with different chelating agents [EDTA, NTA (nitrilotriacetic acid), citrate, isocitrate] and varying concentrations of Fe2+ and Fe3+ showed that photosynthetic growth and nitrogenase activity of R. rubrum were strongly influenced by the iron supply. It is concluded that EDTA enhanced H2 photoproduction by (I) inhibition of biosynthesis of Hup hydrogenase and (II) mobilization of iron, thereby activating the biosynthesis of the nitrogenase complex.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00180976
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