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  • 1
    Electronic Resource
    Electronic Resource
    Aciculin and its relation to dystrophin: immunocytochemical studies in human normal and Duchenne dystrophy quadriceps muscles (2000)
    Springer
    Acta neuropathologica 99 (2000), S. 654-662 
    Details
    ISSN: 1432-0533
    Keywords: Key words Aciculin ; Dystrophin ; Binding site ; Normal and dystrophic muscles ; Ultrastructural ¶localization
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Aciculin is a novel adherens junction antigen extracted from human uterine smooth muscle that is reported to associate biochemically with dystrophin. We attempted to determine (i) the immunostainability of anti-aciculin antibody for the 6 histochemically normal human muscles and seven muscles from boys with Duchenne muscular dystrophy(DMD) and 11 disease control muscles, (ii) the ultrastructural localization of aciculin in normal skeletal myofibers, (iii) aciculin’s spacial relationship with dystrophin and β-spectrin, and (iv) if the aciculin is ultrastructurally colocalized with dystrophin, the distance from the aciculin epitope to the epitope of the dystrophin N- or C-terminal domain. For this, rabbit anti-aciculin antibody was generated against the synthetic peptide of aciculin fragment D [4]. Immunohistochemical staining showed that the immunostainability of DMD muscles for anti-aciculin antibody was markedly decreased as compared with normal and disease control muscles. Single and double immunogold labeling electron microscopy of 6 histochemically normal human quadriceps femoris muscles revealed that aciculin was present along the inner surface of muscle plasma membrane and that aciculin formed doublets more frequently with dystrophin (23.5 ± 1.8%; group mean ± SE) than with β-spectrin (12.8 ± 1.1%; P 〈 0.01 two tailed t test). Rabbit anti-aciculin antibody frequently formed doublets with monoclonal antibodies against the N- or C-terminal domain of dystrophin at the muscle cell surface. These results suggest that aciculin is associated with dystrophin and may interact with both the N- and C-terminal domains of dystrophin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004010051176
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  • 2
    Electronic Resource
    Electronic Resource
    Kinetics of gelatinization of cornstarch adhesive (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Applied Polymer Science 31 (1986), S. 2779-2789 
    Details
    ISSN: 0021-8995
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Notes: In the manufacture of corrugated board, thermal gelatinization of raw starch granules in the adhesive is essential for bonding setting. Kinetic studies of gelatinization of cornstarch adhesive under conditions simulating those at the corrugator revealed that the rate of advance of the gelatinization front in the starch film was linear with square root of time. A quasiactivation energy of 35.5 kJ/mol was found. The gelatinization process, above the gel point, was controlled by the rate of diffusion of water into the starch granules.
    Additional Material: 12 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/app.1986.070310831
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Conductivity and water sorption in paper (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Applied Polymer Science 30 (1985), S. 1257-1266 
    Details
    ISSN: 0021-8995
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Notes: Under equilibrium conditions the dependence of the electrical conductivity of cotton cellulose (Whatman 42 ashless filter paper) on moisture content was of an exponential type up to 3.5%. The transient conductivity of paper undergoing water sorption has been measured concurrently with the transient moisture content. The transient conductivity was greater than that at steady state, the difference increasing with decreasing initial moisture content. The results are explained in terms of thermal effects due to the heat evolved during water sorption.
    Additional Material: 11 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/app.1985.070300329
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    Paper (German National Licenses)
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