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  • 1
    Monograph available for loan
    Monograph available for loan
    The role of magentism in climate (1987)
    Montreal : Nomos Intersc.
    Details Availability
    Call number: MOP 45003
    Type of Medium: Monograph available for loan
    Pages: 13 S.
    Series Statement: Internal Report 1987, 03
    Location: MOP - must be ordered
    Branch Library: GFZ Library
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  • 2
    Electronic Resource
    Electronic Resource
    Endospores of Sporosarcina halophila: characteristics and ultrastructure (1985)
    Springer
    Archives of microbiology 140 (1985), S. 338-342 
    Details
    ISSN: 1432-072X
    Keywords: Sporosarcina halophila ; Endospores ; Electron microscopy ; Heat resistance ; Ethanol resistance ; Germination ; Dipicolinic acid
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Sporosarcina halophila forms endospores. Electron micrographs revealed ultrastructural similarity to spores of S. ureae. Spore germination indicated by loss of refractility, darkening, swelling and formation of new vegetative cells was followed by phase contrast light microscopy. To induce spore germination, the endospores needed to be heat avtivated. After activation, they were inoculated into nutrient broth medium supplemented with sea-water. Double concentrated sea-water was found to be optimal for germination. Similar to other bacterial endospores, the spores were found to be resistant to heat and ethanol. An ultraviolet absorbing substance was isolated from suspensions of free spores; it was identified to be pyridine-2,6-dicarboxylic acid (DPA) usually present in bacterial spores. DPA was detected in amounts ranging from 5–7% of the spore dry weight; it was not detected in extracts of vegetative cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00446974
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  • 3
    Electronic Resource
    Electronic Resource
    Immunocytochemical localization of proteins P1, P2, P3 of glycine decarboxylase and of the selenoprotein PA of glycine reductase, all involved in anaerobic glycine metabolism of Eubacterium acidaminophilum (1989)
    Springer
    Archives of microbiology 152 (1989), S. 182-188 
    Details
    ISSN: 1432-072X
    Keywords: Glycine decarboxylase ; Glycine reductase ; Lipoamide dehydrogenase ; Selenoprotein PA ; Eubacterium acidaminophilum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Antibodies raised against the glycine decarboxylase proteins P1, P2, P3, and the selenoprotein PA, a component of the glycine reductase complex, were used for immunocytochemical localization experiments. Cells of Eubacterium acidaminophilum from logarithmic growth phase were fixed in the growth media with paraformaldehyde and glutaraldehyde. Fixed cells were embedded by the low-temperature procedure using Lowicryl K4M resin, and the protein A-gold technique was applied for the localization experiments. The vicinity of the cytoplasmic membrane contained about 27% of all gold particles when proteins P1 and P2 were to be localized, 50% for protein PA, and 61% for protein P3. Double immunocytochemical labeling experiments gave evidence for the existence of a protein P1/P2 complex located predominantly in the cytoplasm, and a P3/PA complex located at the cytoplasmic membrane. Only in very few instances the labels for proteins P3 and P1 were seen very close together in respective doublelabeling experiments. These results indicate that glycine decarboxylase does not occur in this organism as a complex consisting of all four proteins, but that protein P3, the atypical lipoamide dehydrogenase, takes part in both the glycine decarboxylase as well as in the glycine reductase reaction.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00456099
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  • 4
    Electronic Resource
    Electronic Resource
    Methane formation from methanol and molecular hydrogen by protoplasts of new methanogenic isolates and inhibition by dicyckohexylcarbodiimide (1986)
    Springer
    Archives of microbiology 146 (1986), S. 245-249 
    Details
    ISSN: 1432-072X
    Keywords: Methanogenic bacteria ; Cell wall ; Protoplasts ; Uncouplers ; Bioenergetics of methanogens ; DCCD and TCS, effect of
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Protoplasts have been prepared by pronase treatment of cells of two as yet unidentified methanogenic species, strains Gö1 and AJ2. The rate in which these protoplasts formed methane from methanol and molecular hydrogen amounted to 55% (strain Gö1) or 18% (strain AJ2) of the rate of whole cells. Cell extracts, however, had lost most of the activity, and the rate was only 3.6% of the one of whole cells. Methanogenesis by protoplasts from the above mentioned substrates was inhibited by dicyclohexylcarbodiimide, and this inhibition could be abolished by the protonophore tetrachlorosalicylanilide.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00403224
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  • 5
    Electronic Resource
    Electronic Resource
    Localization and immunological characterization of the cellulolytic enzyme system in Clostridium thermocellum (1989)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 61 (1989), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract The cellulolytic enzyme complex from Clostridium thermocellum JW 20 was purified from the cellulose to which the enzyme was bound during growth. After centrifugation and gel filtration the enzyme complex was analyzed by SDS-PAGE. Three subunits with apparent molecular weights of 195 000 Da, 97 000 Da and 72 000 Da were purified by preparative SDS-PAGE and electroelution. Polyclonal antibodies directed against these three subunits were raised in rabbits. The specificity of the antisera was tested with immunochemical methods. Cross reactions with other subunits of the cellulase complex were observed. Immunoelectron microscopy of protein-A gold labeled, resin embedded cells indicated that the three types of subunits were located in the outer region of the cytoplasm and on structures at the outside of the cell wall.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1989.tb03554.x
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  • 6
    Electronic Resource
    Electronic Resource
    Attachment of CO dehydrogenase to the cytoplasmic membrane is limiting the respiratory rate of Pseudomonas carboxydovorans (1985)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 28 (1985), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Cells of Pseudomonas carboxydovorans from the exponential growth phase revealed the major portion (87%) of CO dehydrogenase attached to the inner aspect of the cytoplasmic membrane. In stationary cells only about half of the total amount of the enzyme remained membrane-bound, and a drop of the CO-oxidizing activity with O2 was observed. The CO-oxidizing activity with the unphysiological electron acceptor methylene blue, which does not need any contact of the enzyme with the membrane, always exceeded that with O2. Measurements of respiration rates of extracts with different electron donors in addition to CO suggested that the electron transport chain is not rate-limiting. It is concluded that the electron flow from CO to O2 in intact cells of P. carboxydovorans is controlled by the amount of CO dehydrogenase attached to a membrane-bound electron acceptor.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1985.tb00780.x
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  • 7
    Electronic Resource
    Electronic Resource
    Plasma production by laser-driven explosively heated thin metal films (1985)
    [S.l.] : American Institute of Physics (AIP)
    Journal of Applied Physics 57 (1985), S. 827-829 
    Details
    ISSN: 1089-7550
    Source: AIP Digital Archive
    Topics: Physics
    Notes: A simple method of producing a relatively large volume of metal vapor for laser-plasma interaction studies is described. The method uses the explosive removal of a thin metal film from a glass substrate with a low-intensity laser pulse.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.334733
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  • 8
    Electronic Resource
    Electronic Resource
    Localization of the membrane-bound hydrogenase in Alcaligenes eutrophus by electron microscopic immunocytochemistry (1988)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 50 (1988), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract The membrane-bound hydrogenase was localized in cells of Alcaligenes eutrophus by electron microscopic immunocytochemistry. Post-embedding labeling performed on ultrathin sections revealed that the enzyme was located predominantly (80%) at the cell periphery in autotrophically and heterotrophically grown bacteria harvested from the exponential phase of growth. In the stationary growth phase, however, only 50% of the enzyme was found at the cell periphery; the remaining 50% was distributed over the cytoplasm. The relative amount of electron microscopic label per cell as seen by application of the protein A—gold technique was higher in cells grown autotrophically as compared to cells grown heterotrophically on fructose. Derepression of the enzyme was followed electron microscopically in a substrate-shift experiment (growth on fructose, followed by a shift to glycerol). Major amounts of the enzyme appeared to undergo a reattachment to the cytoplasmic membrane under these conditions, starting with a reduced location of the enzyme in the cytoplasm and an accumulation in cell areas close to the cytoplasmic membrane. These findings indicate that the ‘membrane-bound’ hydrogenase (i.e., that material enriched as membrane-bound enzyme according to the appropriate activity test) is not, in fact, membrane bound or membrane integrated but membrane associated. It may or may not interact with the cytoplasmic face of the cytoplasmic membrane, depending on the growth phase and conditions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1988.tb02949.x
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  • 9
    Electronic Resource
    Electronic Resource
    Changes in the cell envelope structure of Clostridium sp. strain EM1 during massive production of α-amylase and pullulanase (1987)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 41 (1987), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Marked changes in cell envelope structure were observed when Clostridium sp. strain EM1 cells grown in continuous culture under glucose limitation were compared with cells grown under starch limitation. The increase in the level of extracellular α-amylase and pullulanase during starch-limited growth was parallelled by degradation of the cell-envelope layer and the formation of blebs and a high number of vesicles, which apparently originated from the cytoplasmic membrane. These vesicles were covered by a delicate layer of small particles and were shown to be released into the culture fluid. It is assumed that the overproduction of enzyme destined to remain associated with the cells led to these changes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1987.tb02195.x
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  • 10
    Electronic Resource
    Electronic Resource
    Structure of D-ribulose-l,5-bisphosphate carboxylase/oxygenase from Alcaligenes eutrophyus H16 (1987)
    [s.l.] : Nature Publishing Group
    Nature 325 (1987), S. 730-732 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] A variety of approaches to analysing the major structural aspects of the tobacco and the A. eutrophus RuBPCase have led to the consensus that the molecule has an L8S8 stoichiometry, a diameter of around 125 A and a height of around 100 A. These studies include electron microscopy of negatively ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/325730a0
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