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  • Articles  (19)
  • Electron microscopy  (7)
  • Nitrate reductase  (7)
  • 21.10.Re  (5)
  • Springer  (19)
  • American Institute of Physics
  • Nature Publishing Group
  • Springer Nature
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  • Articles  (19)
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  • Springer  (19)
  • American Institute of Physics
  • Nature Publishing Group
  • Springer Nature
  • Elsevier  (3)
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  • 1
    Electronic Resource
    Electronic Resource
    New results on the superdeformed band in192Hg (1994)
    Springer
    The European physical journal 347 (1994), S. 223-224 
    Details
    ISSN: 1434-601X
    Keywords: 21.10.Re ; 23.20.Lv ; 27.80.+w
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Abstract New results on the192Hg superdeformed band have been obtained with EUROGAM. The experiment has been performed with the160Gd(36S,4n) reaction at 159 MeV. Above 800 keV the γ-ray energies differ from the previously published ones. Thus the rise of the dynamical moment of inertia $$\mathfrak{F}^{(2)} $$ above ħω=0.4 MeV is no longer observed. This is in better agreement with recent cranked Hartree-Fock-Bogoliubov calculations.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01292380
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  • 2
    Electronic Resource
    Electronic Resource
    First evidence of the magnetic character of dipole transitions in the “oblate bands” of199Pb (1994)
    Springer
    The European physical journal 347 (1994), S. 289-290 
    Details
    ISSN: 1434-601X
    Keywords: 21.10.Re ; 23.20.Lv ; 27.80+w
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Abstract Internal conversion coefficients have been determined from online measurement of electron- and y- ray emission related to the dipole transitions in the so-called oblate collective bands in 199Pb.The results strongly support the M1 (or M1+E2) character of these transitions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01289799
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  • 3
    Electronic Resource
    Electronic Resource
    First observation of a superdeformed nucleus produced in an α xn reaction channel (1994)
    Springer
    The European physical journal 349 (1994), S. 5-6 
    Details
    ISSN: 1434-601X
    Keywords: 21.10.Re ; 23.20.Lv ; 27.80.+w
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Abstract Recent data from the EUROGAM array have revealed the population of the yrast superdeformed (SD) band of192Hg in the α4n exit channel of the16O+184W reaction at 113 MeV beam energy. The nucleus assignment was made on the basis of the SD band transition energies, and the observation of characteristic X-rays and lowlying yrast γ-transition of192Hg in coincidence with the SD band γ-rays. Both the feeding and decay-out patterns of the observed SD band have been found similar to the ones previously measured in the (36S,4n) reaction.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01296325
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  • 4
    Electronic Resource
    Electronic Resource
    Freeze fracture studies of reaction centers from Rhodospirillum rubrum in chromatophores and liposomes (1981)
    Springer
    Archives of microbiology 130 (1981), S. 125-128 
    Details
    ISSN: 1432-072X
    Keywords: Rhodospirillum rubrum ; Chromatophores ; Reaction centers ; Liposomes ; Electron microscopy
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract In freeze-fractures of chromatophores of Rhodospirillum rubrum the reaction centers are seen as hexagonal arranged particles of 13 nm diameter with a density of around 5,500 particles per μm2. Similar regions on the cytoplasmic membrane suggest that these parts are the prospective invagination sites. Isolated reaction centers are easily incorporated into liposomes. In freeze fractures of liposomes particles similar in shape and size, although less dense as in chromatophores are observed. In negative staining much smaller units of only 5 nm in diameter are found indicating that reaction centers occur in the membrane as tri- or tetramers. There is a strong correlation between particle density in chromatophores and titratable reaction centers remaining in these membranes after extraction of reaction centers by detergents; both values are in good agreement with the yield of reaction centers at a given detergent concentration.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00411063
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  • 5
    Electronic Resource
    Electronic Resource
    The periplasmic nitrate reductase of Rhodobacter capsulatus; purification, characterisation and distinction from a single reductase for trimethylamine-N-oxide, dimethylsulphoxide and chlorate (1987)
    Springer
    Archives of microbiology 147 (1987), S. 340-345 
    Details
    ISSN: 1432-072X
    Keywords: Rhodobacter capsulatus ; Periplasmic enzymes ; Nitrate reductase ; Trimethylamine-N-oxide/dimethylsulphoxide/chlorate reductase ; Molybdenum cofactor
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The periplasmic dissimilatory nitrate reductase from Rhodobacter capsulatus N22DNAR+ has been purified. It comprises a single type of polypeptide chain with subunit molecular weight 90,000 and does not contain heme. Chlorate is not an alternative substrate. A molybdenum cofactor, of the pterin type found in both nitrate reductases and molybdoenzymes from various sources, is present in nitrate reductase from R. capsulatus at an approximate stoichiometry of 1 molecule per polypeptide chain. This is the first report of the occurrence of the cofactor in a periplasmic enzyme. Trimethylamine-N-oxide reductase activity was fractionated by ion exchange chromatography of periplasmic proteins. The fractionated material was active towards dimethylsulphoxide, chlorate and methionine sulphoxide, but not nitrate. A catalytic polypeptide of molecular weight 46,000 was identified by staining for trimethylamine-N-oxide reductase activity after polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulphate. The same polypeptide also stained for dimethylsulphoxide reductase activity which indicates that trimethylamine-N-oxide and dimethylsulphoxide share a common reductase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00406130
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  • 6
    Electronic Resource
    Electronic Resource
    R-Bodies in newly isolated free-living hydrogen-oxidizing bacteria (1979)
    Springer
    Archives of microbiology 121 (1979), S. 9-15 
    Details
    ISSN: 1432-072X
    Keywords: R-Bodies ; Kappa particles ; Free-living hydrogen bacteria ; Induction ; Electron microscopy ; Chemical composition ; Defective prophages ; Plasmids
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract R-Bodies have been found in a recently isolated pseudomonas-like free-living hydrogen oxidizing bacterium. Their isolation, fine structure and chemical composition are described and compared with the R-bodies from the kappa particles (Caedobacter), obligate endosymbionts of Paramecium aurelia. The 2K 1 R-bodies exhibited essential characteristics of the kappa R-bodies; however, their size and some other structural aspects proved that they represent a new type of R-bodies. The presence of phage tail-like particles in cells induced with Mitomycin C is in favour of the hypothesis that the R-bodies might be coded by defective prophages, or by extrachromosomal elements.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00409199
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  • 7
    Electronic Resource
    Electronic Resource
    Membrane-bound nitrite oxidoreductase of Nitrobacter: evidence for a nitrate reductase system (1984)
    Springer
    Archives of microbiology 140 (1984), S. 153-158 
    Details
    ISSN: 1432-072X
    Keywords: Nitrobacter hamburgensis ; Nitrite oxidoreductase ; Nitrate reductase ; Molybdenum iron-sulfur protein ; Ultrastructure
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Nitrite oxidoreductase, the essential enzyme complex of nitrite oxidizing membranes, was isolated from cells of the nitrifying bacterium Nitrobacter hamburgensis. The enzyme system was solubilized and purified in the presence of 0.25% sodium deoxycholate. Nitrite oxidoreductase oxidized nitrite to nitrate in the presence of ferricyanide. The pH optimum was 8.0, and the apparent K m value for nitrite amounted to 3.6 mM. With reduced methyl-and benzylviologen nitrite oxidoreductase exhibited nitrate reductase activity with an apparent K m value of 0.9 mM for nitrate. NADH was also a suitable electron donor for nitrate reduction. The pH optimum was 7.0. Treatment with SDS resulted in the dissociation into 3 subunits of 116,000, 65,000 and 32,000. The enzyme complex contained iron, molydbenum, sulfur and copper. A c-type cytochrome was present. Isolated nitrite oxidoreductase is a particle of 95±30 Å in diameter.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00454918
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  • 8
    Electronic Resource
    Electronic Resource
    Bradyrhizobium japonicum mutants defective in root-nodule bacteroid development and nitrogen fixation (1986)
    Springer
    Archives of microbiology 144 (1986), S. 355-366 
    Details
    ISSN: 1432-072X
    Keywords: Bradyrhizobium ; Electron microscopy ; Mutants ; Nitrogen fixation ; Nodulation ; Soybean ; Symbiosis ; Transposon Tn5
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The genome of the slow-growing Bradyrhizobium japonicum (strain 110) was mutagenized with transposon Tn5. A total of 1623 kanamycin/streptomycin resistant derivatives were screened in soybean infection tests for nodulation (Nod) and symbiotic nitrogen fixation (Fix). In this report we describe 14 strains possessing a stable, reproducible Nod+Fix- phenotype. These strains were also grown under microaerobic culture conditions to test them for free-living nitrogen fixation activity (Nif). In addition to strains having reduced Fix and Nif activities, there were also strains that had reduced symbiotic Fix activity but were Nif+ ex planta. Analysis of the genomic structure revealed that the majority of the strains had a single Tn5 insertion without any further apparent physical alteration. A few strains had additional insertions (by Tn5 or IS50), or a deletion, or had cointegrated part of the vector used for Tn5 mutagenesis. One of the insertions was found in a known nif gene (nifD) whereas all other mutations seem to affect different, hitherto unknown genes or operons. Several mutant strains had an altered nodulation phenotype, inducing numerous, small, widely distributed nodules. Light and electron microscopy revealed that most of these mutants were defective in different stages of bacteroid development and/or bacteroid persistence. The protein patterns of the mutants were inspected by two-dimensional gel electrophoresis after labelling microaerobic cultures with l-(35S)methionine. Of particular interest were mutants lacking a group of proteins the synthesis of which was known to be under oxygen control. Such strains can be regarded as potential regulatory mutants.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00409885
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  • 9
    Electronic Resource
    Electronic Resource
    Immature rat epididymal epithelial cells grown in static primary monolayer culture on permeable supports (1989)
    Springer
    Cell & tissue research 256 (1989), S. 573-580 
    Details
    ISSN: 1432-0878
    Keywords: Epididymis ; Epithelium ; Monolayer culture ; Histochemistry ; Electron microscopy ; Rat (Sprague-Dawley)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary N-acetylglucosaminidase (NAG), acid phosphatase (ACP) and alkaline phosphatase (AKP) were localised histochemically in fixed cells from the 37-day-old rat epididymis grown in static monolayer culture for 2–8 days. ACP and NAG were cytosolic enzymes found in perinuclear positions, whereas staining of AKP was consistent with a membranous position. These enzymes were also examined in frozen tissue sections of the epididymis, from rats of the equivalent age, where NAG had intense activity in both supra- and infra-nuclear cytoplasm and ACP was more active apically. For the first time AKP was localised along basolateral membranes of the epithelium and in the lumen of the mid-caput region. The monolayer in culture was of principal cells only and they maintained their polarity and ultrastructural characteristics, but the height of the cells was reduced compared to that obtained in situ.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00225606
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  • 10
    Electronic Resource
    Electronic Resource
    Cloning of DNA fragments complementary to tobacco nitrate reductase mRNA and encoding epitopes common to the nitrate reductases from higher plants (1987)
    Springer
    Molecular genetics and genomics 209 (1987), S. 552-562 
    Details
    ISSN: 1617-4623
    Keywords: Nitrate reductase ; cDNA expression cloning ; Tobacco ; Sequence ; Cytochrome b5
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Messenger RNAs encoding the nitrate reductase apoenzyme from tobacco can be translated in a cell-free system. Poly(A)+ mRNA fractions from the 23-32 S area of a sucrose gradient were used to build a cDNA library in the expression vector λgt11 with an efficiency of cloning of approximately 104 recombinants/ng mRNA. Recombinant clones were screened with a rabbit polyclonal antibody directed against the corn nitrate reductase, which cross reacts specifically with the nitrate reductases from dicotyledons. Among 240000 recombinant plaques, eight clones were isolated containing inserts of sizes ranging from 1.6 kb to 2.1 kb and sharing sequence homologies. Seven of these clones contained a common internal 1.6 kb EcoRI fragment. The identity of these clones was confirmed as follows. A fusion protein of 170 kDa inducible by IPTG and recognized by the rabbit nitrate reductase antibody was expressed by a lysogen derived from one of the recombinants. The antibodies binding the fused protein were eluted and shown to be inhibitory to the catalytic activity of tobacco nitrate reductase. Two monoclonal antibodies directed against nitrate reductase were also able to bind the hybrid protein. The 1.6 kb EcoRI fragment was sequenced by the method of Sanger. The open reading frame corresponding to a translational fusion with the β-galactosidase coding sequence of the vector shared strong homology at the amino acid level with the heme-binding domain of proteins of the cytochrome b5 superfamily and with human erythrocyte cytochrome b5 reductase. When the 1.6 kb EcoRI fragment was used as a probe for Northern blot experiments a signal corresponding to a 3.5 kb RNA was detected in tobacco and in Nicotiana plumbaginifolia mRNA preparations but no cross-hybridization with corn mRNAs was detected. The probe hybridized with low copy number sequences in genomic blots of tobacco DNA.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00331162
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