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  • 1
    Book
    Book
    Geochemistry of Clay-pore Fluid Interactions (1993)
    London [u.a.] : Chapman & Hall
    Details Availability
    Keywords: Geology and Palaeontology ; Soil mechanics Congresses ; Clay Congresses ; Geochemistry Congresses ; Fluid dynamics Congresses ; Kongreß Konferenz ; soil mechanics ; clay ; geochemistry ; fluid dynamics ; Konferenzschrift ; Tonmineralogie ; Geochemie ; Tonmineral ; Porosität ; Abdichtung ; Barriere ; Speichergestein ; Ton ; Strömungsmechanik ; Ton
    Type of Medium: Book
    Pages: XV, 427 S. , graph.Darst.
    Edition: 1.ed.
    ISBN: 0412489805
    Series Statement: The Mineralogical Society series 4
    URL: http://www.loc.gov/catdir/enhancements/fy0822/92039558-d.html
    URL: http://digitale-objekte.hbz-nrw.de/webclient/DeliveryManager?pid=2582793&custom_att_2=simple_viewer
    DDC: 551.9
    RVK:
    RB 10115
    Language: English
    Note: Literaturangaben
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  • 2
    Electronic Resource
    Electronic Resource
    High frequency capillary waves: A light scattering spectrometer (1993)
    [S.l.] : American Institute of Physics (AIP)
    Review of Scientific Instruments 64 (1993), S. 2789-2795 
    Details
    ISSN: 1089-7623
    Source: AIP Digital Archive
    Topics: Physics , Electrical Engineering, Measurement and Control Technology
    Notes: Modifications to a light scattering apparatus to permit study of liquid surface fluctuations of significantly higher wave number than hitherto are described. Various problems associated with the modified system are discussed. Typical results are presented for capillary wave propagation on the surface of two different fluids, demonstrating the satisfactory functioning of the spectrometer despite these problems.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.1144364
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  • 3
    Electronic Resource
    Electronic Resource
    Vacuum ultraviolet excitation of large water clusters (1994)
    s.l. : American Chemical Society
    The @journal of physical chemistry 〈Washington, DC〉 98 (1994), S. 12530-12534 
    Details
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/j100099a015
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  • 4
    Electronic Resource
    Electronic Resource
    High-frequency capillary waves on the clean surface of water (1991)
    s.l. : American Chemical Society
    Langmuir 7 (1991), S. 2419-2421 
    Details
    ISSN: 1520-5827
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/la00059a002
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  • 5
    Electronic Resource
    Electronic Resource
    The Endothelial Cell as a Regulator of T-Cell Function (1990)
    Oxford, UK : Blackwell Publishing Ltd
    Immunological reviews 117 (1990), S. 0 
    Details
    ISSN: 1600-065X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1600-065X.1990.tb00568.x
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  • 6
    Electronic Resource
    Electronic Resource
    Isolation of the Actinobacillus pleuropneumoniae haemolysin gene and the activation and secretion of the prohaemolysin by the HlyC, HlyB and HlyD proteins of Escherichia coli (1990)
    Oxford, UK : Blackwell Publishing Ltd
    Molecular microbiology 4 (1990), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: The gene encoding the c. 105 kD secreted haemolysin protein of the porcine pathogen Actinobacillus pleuropneumoniae serotype 1 has been isolated by screening a lambda gt11 expression library in Escherichia coli with antiserum raised against the wild-type protein. A derivative recombinant DNA pJFF702 expressed the hlylA haemolysin gene from the pUC19 lac promoter but the resulting haemolysin I protein remained within the E. coli cell and was haemolytically inactive. Export of the intracellular A. pleuropneumoniae prohaemolysin out into the medium was achieved by the presence in trans of the E. coli haemolysin secretion genes hlyB and hlyD, and high levels of intracellular haemotytic activity were attained similarly by the E. coli post-translational haemolysin activator gene, hlyC. Southern hybridization of A. pleuropneumoniae parental DNA nevertheless indicated only a low degree of nucleotide sequence identity to the haemolysin structural and secretion genes hlyA and hlyB of E. coli. The data show that despite substantial nucleotide sequence divergence the A. pleuropneumoniae serotype 1 haemolysin determinant is closely related to that which is dispersed throughout other Gram-negative human and animal pathogens.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2958.1990.tb02021.x
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  • 7
    Electronic Resource
    Electronic Resource
    Closely linked genetic loci required for swarm cell differentiation and multicellular migration by Proteus mirabilis (1991)
    Oxford, UK : Blackwell Publishing Ltd
    Molecular microbiology 5 (1991), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: The pathogenic bacterium Proteus mirabilis exhibits a form of multicellular behaviour called swarming migration. This involves the differentiation of vegetative cells at the colony margin into swarm cells which are long, aseptate, multinucleate, hyper-flagellated filaments able to undergo repeated cycles of co-ordinated population migration and consolidation (reversion to vegetative cells). Transposon mutagenesis of uropathogenic P. mirabilis strain U6450 with Tn5 generated 4860 chromosomal insertions and, of these, 75 (1.6%) caused visibly abnormal swarming behaviour, indicating that at least 45 genes are involved in directing motility, cell differentiation and multicellular behaviour. While about one fifth of the swarm-defective mutants lacked flagella and were non-motile non-swarming (NMNS) the majority were normally flagellated and motile but were unable to form swarm cells (motile non-swarming, MNS), or were motile and able to form swarm cells but displayed abberant patterns of multicellular migration (dendritic swarming, DS) or consolidation (frequent and infrequent consolidation, FC and IC). Restriction enzyme mapping of representative mutant DNAs by Southern hybridization with transposon DNA probes identified eight different mutated genetic loci within the five phenotypic classes. Subsequent Southern analysis of large restriction fragments separated by pulsed-field electrophoresis showed that these eight mutated loci required for motility, cell differentiation and multicellular migration were clustered on a region of DNA spanning approximately 8% of the 4.2mbp P. mirabilis chromosome. Further linkage analysis showed that the DS locus involved in the ordered migration of the swarm cell population mapped separately from two main clusters of swarm loci, one cluster containing, within 112kbp, genetic determinants of motility (NMNS) and also differentiation into swarm cells (MNS1, MNS2), and second within aneighbouring 95kbp DNA sequence containing three loci involved in the control of consolidation (FC, IC1, IC2).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2958.1991.tb00819.x
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  • 8
    Electronic Resource
    Electronic Resource
    Mutational analysis supports a role for multiple structural features in the C-terminal secretion signal of Escherichia coli haemolysin (1991)
    Oxford, UK : Blackwell Publishing Ltd
    Molecular microbiology 5 (1991), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: We have carried out an extensive mutational analysis of the C-terminal signal which targets the export of the 1024-residue haemolysin protein (HlyA) of Escherichia coli across both bacterial membranes into the surrounding medium. Over 60 variants of the HlyA C-terminal 53-amino-acid sequence were created by oligonucleotide-directed mutagenesis and fused to the HlyA N-terminal 830 residues. Transport of the HlyA derivatives by the HlyB/HlyO system was compared with the wild-type level and the data indicate that the HlyA C-terminal export signal lies within the last 48 amino acids and comprises three functional domains: an amphipathic, charged helix between residues 1,977 and R,996; a 13-amino-acid uncharged region from residue T,997 to S,1009; and an 8-aminoacid hydroxylated tail at the extreme C-terminus. Analogous features were found in the C-terminal sequences of an extended family of haemolysins, leukotoxins and proteases which are secreted by HlyB/HlyD-type translocators. In particular, all nine proteins which are secreted into the extracellular medium possess potential extended amphipathic helices. These results suggest a possible role for multiple regions of the HlyA C-terminal export signal in which the first two domains span the membranes and the third domain remains in the cytoplasm.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2958.1991.tb02085.x
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  • 9
    Electronic Resource
    Electronic Resource
    In vitro activation of Escherichia coli prohaemolysin to the mature membrane-targeted toxin requires HlyC and a low molecular-weight cytosolic polypeptide (1991)
    Oxford, UK : Blackwell Publishing Ltd
    Molecular microbiology 5 (1991), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: The c. 110kDa haemolysin toxin secreted by Escherichia coli and other pathogenic Gram-negative bacteria is synthesized as the non-toxic precursor, prohaemolysin (proHlyA), which is unable to target mammalian cell membranes until activated intracellularly by an unknown mechanism dependent upon the coexpressed c. 20kDa protein, HlyC. We have established in vitro post-translational activation of proHlyA in membrane-depleted cell extract fractions from E. coli recombinant strains containing (separately) the proHlyA and HlyC proteins. In vitro activation was calcium-independent and effective over a pH range of 6 to 9 and at temperatures from 42°C to 4°C. HlyC cell extract was also able to activate proHlyA which had been secreted out of cells containing the export proteins HlyB and HlyD. Fractionation of HlyC cell extracts by sucrose gradient centrifugation and molecular weight chromatography revealed activating fractions as having a molecular mass of 40kDa, suggesting that the HlyC activator is present physiologically in a multimeric form. Cell extracts containing activation-competent HlyC and proHlyA were inactive following dialysis, but activity was restored by complementation with a cell extract lacking both proteins. HlyC and proHlyA proteins which were overproduced separately from recombinant expression plasmids were inactive following purification, but activity could again be restored with a Hly-negative cell extract. These experiments demonstrated that HlyC is not sufficient for activation; an additional cellular factor is required. The cellular factor was found in enterobacteria but not other bacteria or eukaryotic cells. It was cytosolic, protease-sensitive, and behaved as a c. 10kDa polypeptide in a number of assays including dialysis, sucrose gradient centrifugation, and gel filtration chromatography. Thus activation was possible in a defined in vitro reaction containing only purified proHlyA, HlyC, and the cellular factor. Ki stic studies in which the relative concentrations of the three components of proHlyA activation were varied suggested that neither HlyC nor the cellular factor acts as a conventional enzyme, with each participating in a finite number of activation events.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2958.1991.tb01914.x
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  • 10
    Electronic Resource
    Electronic Resource
    Nutritional improvement of the aspartate family of amino acids in edible crop plants (1993)
    Springer
    Amino acids 4 (1993), S. 21-34 
    Details
    ISSN: 1438-2199
    Keywords: Amino acids ; Lysine ; Methionine ; Nutritional improvement ; Aspartokinase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Plants are the primary source of protein for man and livestock, however, not all plants produce proteins which contain a balance of amino acids for the diet to ensure proper growth of livestock and humans. Alteration of the amino acid composition of plants may be accomplished using techniques of molecular biology and genetic engineering. Genes encoding key enzymes regulating the synthesis of lysine and threonine have been cloned from plants andE. coli and are available for modification and transformation into plants. Genes encoding seed storage proteins have been cloned and modified to encode more lysine residues for developing transgenic plants with higher seed lysine. Genes encoding seed storage proteins naturally higher in methionine have been cloned and expressed in transgenic plants, increasing methionine levels of the seed. These and other approaches hold great promise in their application to increasing the content of essential amino acids in plants.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00805798
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