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  • 1
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    Unknown
    Berlin : Periodicals Archive Online (PAO)
    Deutsche Zeitschrift für Philosophie. 4:2 (1956) 246 
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  • 2
    facet.materialart.
    Unknown
    Berlin : Periodicals Archive Online (PAO)
    Deutsche Zeitschrift für Philosophie. 4:2 (1956) 217 
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  • 3
    Electronic Resource
    Electronic Resource
    Weinheim : Wiley-Blackwell
    Angewandte Makromolekulare Chemie 71 (1978), S. 221-226 
    ISSN: 0003-3146
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Description / Table of Contents: Technical urea-formaldehyde resins are almost completely demethylolated on heating with alcaline earth hydroxydes. Higher methylene-bridged oligomers and partially crosslinked materials are precipitated. Methylol groups are not quantitatively removed, as methylolated lower molecular weight oligomers are still present in the aqueous solution. The major amount of liberated formaldehyde is irreversibly converted to hexoses by aldolization.
    Notes: Technische Harnstoff-Formaldehyd-Harze werden in der Wärme durch Einwirkung von Erdalkalihydroxyden weitgehend entmethyloliert, wobei die höhermolekularen methylenverbrückten Oligomeren und bereits teilvernetzte Kondensate ausfallen. Die Abspaltung ist nicht quantitativ, da die Spaltlösung noch niedermolekulare lösliche methylolgruppenhaltige Oligomere enthält. Der freigesetzte Formaldehyd wird hauptsächlich durch Aldolisierung zu Hexosen irreversibel gebunden.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 12 (1979), S. 151-164 
    ISSN: 0091-7419
    Keywords: membrane glycoproteins ; posttranslational modifications ; intracellular transport ; secretion ; Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The early steps in the biosynthesis of glycoproteins associated with the plasma membranes of rat hepatoma tissue culture cells has been analyzed. By measuring the effect of tunicamycin on the incorporation of [3H] mannose and [3H] fucose into cell glycoproteins, it was determined that an interval of about 1 h was required to transfer the glycoprotein from the site of mannosylation to the site of fucosylation. This result was corroborated by an analysis of the time required for the appearance of either mannose or fucose-labeled glycoproteins at the cell surface. The separation of membrane glycoproteins by a two-dimensional gel system allowed the visualization of the modifications leading to both size and charge heterogeneity of these proteins. By following the changes in electrophoretic mobility introduced into membrane glycoproteins during a chase period after a pulse labeling, the time course of these molecular alterations could be estimated. Several glycoproteins have apparently higher rates of synthesis than the bulk of membrane-associated glycoproteins. Most of these glycoproteins were released within 2 h after biosynthesis from the intracellular membrane fraction and appear after 3 h in the medium. In addition to the glycoproteins that contain both mannose and fucose and that show a high degree of charge heterogeneity, there are other membrane-bound species that are not noticeably modified by the in corporation of fucose or sialic acids. These glycoproteins could represent constituents limited to the internal membrane system of the HTC cell.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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