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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
    ESR linewidth broadening of a hydrophobic probe in some surfactant solutions (1984)
    Springer
    Colloid & polymer science 262 (1984), S. 978-981 
    Details
    ISSN: 1435-1536
    Keywords: Micelles ; solubilization ; spin probe ; linewidth broadening ; Poisson distribution
    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 ESR linewidth of tetradecanoyloxy-2,2,6,6-tetramethyl-piperidinyl-l-oxyl was observed in aqueous solutions of hexadecyltrimethylammonium bromide and sodium alkyl (C12 and C14) sulfates at 30 °C. The linewidth increases quadratically with the spin probe concentration to various extents, depending upon micellar properties. The diversity of the linewidth broadening is, however, reduced by plotting the relative linewidth, W/W0, vs. the average solubilization number, m, where W0 is the linewidth at the extremely dilute spin probe concentration. All the experimental points fall on a curve regardless of the diverse micellar properties. The broadening is interpreted in terms of a bimolecular and multimolecular collisions between the spin probes exclusively concentrated in micelles in accordance with the Poisson distribution of the spin probe.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01490030
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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