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  • 1
    Electronic Resource
    Electronic Resource
    Protein substrates and heat shock reduce the DNA-binding ability of Escherichia coli Lon protease (1995)
    Springer
    Applied microbiology and biotechnology 44 (1995), S. 484-488 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Interaction between the fusion protein MBP-Lon, formed by maltose-binding protein and Lon protease, and the plasmid pBR322 was studied to clarify the DNA-binding behavior of the Lon protease. Since the MBP-Lon fusion protein that was bound to the plasmid was strongly adsorbed by amylose resin, complex formation and dissociation were determined by quantifying the unadsorbed plasmid using agarose gel electrophoresis. The autolysis of MBP-Lon fusion protein was suppressed when the protein was bound to the plasmid. The plasmid was completely dissociated from MBP-Lon fusion protein by the addition of the protein substrates of Lon protease (i.e. α-casein and denatured bovine serum albumin). In addition, at high temperatures, MBP-Lon fusion protein lost its plasmid-binding ability, although it fully retained ATP-dependent protease activity. These results suggest that Lon protease loses DNA-binding ability when cells are exposed to abnormal conditions and the amount of damaged proteins increases. On the other hand, DNA probably plays an important role in controlling the Lon protease activity in cells under normal conditions by entrapping the enzyme.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00169948
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  • 2
    Electronic Resource
    Electronic Resource
    Protein substrates and heat shock reduce the DNA-binding ability of Escherichia coli Lon protease (1995)
    Springer
    Applied microbiology and biotechnology 44 (1995), S. 484-488 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract  Interaction between the fusion protein MBP-Lon, formed by maltose-binding protein and Lon protease, and the plasmid pBR322 was studied to clarify the DNA-binding behavior of the Lon protease. Since the MBP-Lon fusion protein that was bound to the plasmid was strongly adsorbed by amylose resin, complex formation and dissociation were determined by quantifying the unadsorbed plasmid using agarose gel electrophoresis. The autolysis of MBP-Lon fusion protein was suppressed when the protein was bound to the plasmid. The plasmid was completely dissociated from MBP-Lon fusion protein by the addition of the protein substrates of Lon protease (i.e. α-casein and denatured bovine serum albumin). In addition, at high temperatures, MBP-Lon fusion protein lost its plasmid-binding ability, although it fully retained ATP-dependent protease activity. These results suggest that Lon protease loses DNA-binding ability when cells are exposed to abnormal conditions and the amount of damaged proteins increases. On the other hand, DNA probably plays an important role in controlling the Lon protease activity in cells under normal conditions by entrapping the enzyme.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002530050586
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  • 3
    Electronic Resource
    Electronic Resource
    Identification of biosynthetic intermediates of the extracellular polysaccharide viilian in Lactococcus lactis subspecies cremoris SBT 0495 (1999)
    Springer
    Archives of microbiology 171 (1999), S. 343-349 
    Details
    ISSN: 1432-072X
    Keywords: Key words Biosynthesis of extracellular ; polysaccharide ; Lipid-linked intermediate ; Lactococci ; Polysaccharide ; Undecaprenol
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Lactococcus lactis subspecies cremoris SBT 0495 produces the phosphopolysaccharide viilian, which consists of the repeating unit β-d-glucosyl-(1→4)-(α-l-rhamnosyl-(1→2))-(α-d-galactose-1-phosphoryl-(→3)-β-galactosyl-(1→4)-β-d-glucose. A lipid extract was prepared from cells in the late exponential phase of growth and was hydrolyzed by hydrochloric acid under mild conditions to split lipid-linked intermediates in the extract into lipid and sugar moieties. Both moieties were purified by chromatographic techniques and were characterized to identify intermediates of the viilian biosynthetic pathway. A polyisoprenoid isolated from the chloroform-soluble fraction of the hydrolyzed lipid extract was identified by mass spectrometry as undecaprenol. Saccharides isolated from the water-soluble fraction of the hydrolyzed lipid extract by anion-exchange chromatography, were characterized by glycosidic linkage analysis to discriminate sugar moieties of intermediates of viilian biosynthesis from compounds liberated from cell wall components. Some oligosaccharide analogues contain a glycerol residue, suggesting that these are fragments of glycosylglycerides and/or lipoteichoic acid. Three fragments were identified to be glucose, galactosyl-(1→4)-glucose, and rhamnosyl-(1→2)-galactosyl-(1→4)-glucose, which are in agreement with the structure of the repeating unit of viilian. These saccharides most likely represent the first three steps of the sequential assembly of the repeating unit of the undecaprenol assembly.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002030050720
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  • 4
    Electronic Resource
    Electronic Resource
    A Box Model of Glacial-Interglacial Variability in the Japan Sea (1999)
    Springer
    Journal of oceanography 55 (1999), S. 483-492 
    Details
    ISSN: 1573-868X
    Keywords: Paleoceanography ; box model ; Japan Sea ; glacial maximum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Geosciences
    Notes: Abstract The Japan Sea has experienced drastic changes in the last 60 ka: the surface water was colder than the present value by five degrees and extremely freshened (∼24 ppt) in the last glacial maximum (∼15 ka), and then it contained Oyashio water for a few thousand years. It is an open question whether the inflow-outflow pattern was entirely reversed, opposite to the present exchange with an inflow through Tsushima Strait and an outflow through Tsugaru Strait. A box model is employed with two boxes representing the northern and the southern half domains in the upper (300-m-thick) layer. The model is driven by atmospheric forcing and inflow through Tsushima Strait and/or Tsugaru Strait. Here, the net transport through Tsushima to Tsugaru is given in the model. A baroclinic component is added to the net transport through each strait. It is the baroclinic components that allow the upper and the lower portions to flow to the opposite directions in the straits, and hence a reversal flow becomes possible against the net transport, under the condition of an extremely freshened Japan Sea. The fresh surface layer in 18∼14 ka is attributable to a near-shutoff of the inflow due to the low sea level. Shortly after the near-shutoff, the baroclinic transport through Tsugaru Strait yields intrusion of the Oyashio water into the Japan Sea. Thus, it is implied that Oyashio water existed in the Japan Sea a few thousand years after the reopening of Tsugaru Strait, even though the net transport was one-way, similar to the present state.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1007831122343
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  • 5
    Electronic Resource
    Electronic Resource
    DNase I interaction on muscle Z-line (1995)
    Springer
    Journal of muscle research and cell motility 16 (1995), S. 123-129 
    Details
    ISSN: 1573-2657
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The effect of deoxyribonuclease I on muscle Z-line structures was re-examined. Under conditions of deoxyribonuclease I activation (presence of the divalent cation Ca2+ and Mg2+), a deoxyribonuclease I preparation did not affect Z-line structure if phenylmethylsulfonylfluoride, an inhibitor of serine proteases, was also present. In the absence of protease inhibitor, both Z-lines and M-lines were digested, even in the presence of EDTA and EGTA as inhibitors of deoxyribonuclease I. These electron microscopic observations were consistent with the following results from sodium dodecyl sulphate gel electrophoresis: when the protease was inhibited but deoxyribonuclease I was activated, myofibrillar proteins remained essentially intact. However, degradation of proteins in both rabbit psoas and chicken pectoralis myofibrils was observed in the presence of deoxyribonuclease I inhibitors when the protease inhibitor was absent. Our data strongly suggest that the interaction of deoxyribonuclease I with Z-line proteins previously reported is most likely due to contamination of the deoxyribonuclease I fraction by the serine-type proteases.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00122530
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