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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Journal of sol gel science and technology 2 (1994), S. 153-156 
    ISSN: 1573-4846
    Keywords: dimethyldiethoxysilane ; oxalic acids ; polydimethylsiloxane ; reaction mechanism ; non-aqueous system
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Polysiloxane formation in dimethyldiethoxysilane (DMDES)-ethyl alcohol (EtOH(D))-oxalic acid (OA) (DMDES:EtOH(D):OA=1:2:0.5) and DMDES-dimethylsulfoxide (DMSO)-OA (DMDES:DMSO:OA=1:2:0.5) systems was investigated by gas chromatography-mass spectrometry and 29Si-nuclear magnetic resonance. While the DMDES-EtOH(D)-OA system was homogeneous, the DMDES-DMSO-OA system consisted of two immiscible phases. In both systems, ethoxy-terminated linear oligomers ((EtO)Me2SiO(Me2SiO)nSiMe2(OEt); n=0–4, Et = C2H5, Me = CH3) and cyclic tetramer ((Me2SiO)4) were identified. The reaction mechanism for polysiloxane formation is discussed.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-8798
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Thirteen monoclonal antibodies (MAbs) to the glycoprotein (G) of vesicular stomatitis virus (VSV) serotype Indiana were prepared and examined for their effects on various biological activities of VSV, including in vitro infection, hemagglutination, adsorption to cells, and mediation of cell fusion. Competitive binding assays with these MAbs revealed the presence of at least seven distinct antigenic determinants (epitopes) on the G protein. In some cases, overlappings among epitopes to various degrees were observed as partial inhibition or binding enhancement. The MAbs to all the epitopes but one (epitopes 1–6) reacted with the denatured G protein in a Western immunoblot analysis. Four of the epitopes (epitopes 2, 4, 5, and 7) were involved in neutralization and two (epitopes 1 and 2) in hemagglutination inhibition. None of the MAbs inhibited the adsorption of radiolabeled VSV to BHK-21 cells; the MAbs to epitope 2 slightly enhanced the virus adsorption. All neutralization epitopes except epitope 2 (epitopes 4, 5, and 7) were associated with inhibition of VSV-mediated cell fusion. These results show a direct spatial relationship between the epitopes recognized by the MAbs and functional sites on G protein and further insights into the structure and function of G protein.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Colloid & polymer science 270 (1992), S. 687-693 
    ISSN: 1435-1536
    Keywords: pHeffect ; ovalbumin ; radius ofgyration ; rheologicalproperties ; SAXS
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
    Notes: Abstract The effect of pH on the molecular shape and dispersed state of native ovalbumin molecules in 20 mM phosphate and acetic acid buffer solutions has been studied using small-angle x-ray scattering (SAXS) and a rheological method The degree of association of the OA molecule at the 0.5% colloid system increases slightly with decreasing pH, i.e., 2.10 at pH 7.0, and 2.88 at pH 4.0, and the radius of the OA molecule decreases slightly with decreasing pH, i.e., 24.5 Å at pH 7.0, and 22.0 Å at pH 4.0. The OA colloid shows apparent yield stress and rigidity which are due to a certain ordered arrangement of the molecules. The yield stress and the rigidity increase abruptly at a pH value near to an isoelectric point (ca. pH 4.4). In the dilute system this increment is attributed to the change in the ordered arrangement or in the interparticle interaction, and not to the change in the association state of the OA molecules. The values of the yield stress and the rigidity remain almost constant over a wide concentration range and this feature (an auto-controlled mechanism) is kept over a certain range of pH.
    Type of Medium: Electronic Resource
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