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  • 1
    Electronic Resource
    Electronic Resource
    Lectin histochemistry of canine polyglucosan bodies (1987)
    Springer
    Acta neuropathologica 73 (1987), S. 177-180 
    Details
    ISSN: 1432-0533
    Keywords: Lectins ; Polyglucosan bodies ; Dog
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Lectin histochemistry was investigated to identify sugar residues of the polyglucosan bodies of canine brain, spinal cord and caecum. The polyglucosan bodies in the brain and spinal cord stained with concanavalin A (ConA) but not with soybean agglutinin, wheat germ agglutinin, peanut agglutinin,Dolichos biflorus agglutinin,Ricinus communis agglutinin andUlex europaeus agglutinin. Caecum, polyglucosan bodies, however, did not stain with any of the seven lectins employed. After periodate oxidation, paradoxical ConA staining was observed in the polyglucosan bodies of the brain, spinal cord and caecum. These results indicate that polyglucosan bodies contain mannose and glucose residues and suggest that the component of polyglucosan bodies is partially derived from rough endoplasmic reticulum, the Golgi apparatus and hypolemmal cisternae.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00693785
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Identification of a cell layer containing α-smooth muscle actin in the connective tissue sheath of human anagen hair (1992)
    Springer
    Archives of dermatological research 284 (1992), S. 246-249 
    Details
    ISSN: 1432-069X
    Keywords: Hair ; Connective tissue sheath ; Alpha-Smooth muscle actin ; Immunohistochemistry ; Immunoelectron microscopy
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Immunohistochemical and immunoelectron microscopy studies revealed the presence of α-smooth muscle (α-SM) actin in fibroblasts located in the connective tissue sheath (CTS) of human anagen hair follicles. Immunostaining was positive from the base of the bulb to the upper part of the lower portion of the mature anagen hair follicles. The late catagen hair follicles did not stain. Ultrastructurally, α-SM actin was detected only in the fibroblasts located in the innermost layer of the transverse collagenous fibres. Since α-SM actin is located in cells with contractile potential, this newly identified layer may play an important role in the morphological changes of the lower portion of the hair follicle during the hair growth cycle.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00375803
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Ionic species produced by mechanical fracture of solid polymer. III. Anions from polytetrafluoroethylene (1987)
    Bognor Regis [u.a.] : Wiley-Blackwell
    Journal of Polymer Science Part B: Polymer Physics 25 (1987), S. 1431-1437 
    Details
    ISSN: 0887-6266
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Notes: The tetracyanoethylene anion radical (\documentclass{article}\pagestyle{empty}\begin{document}${\rm TCNE}^{ \cdot ^ - } $\end{document}) was detected by ESR spectroscopy in polytetrafluoroethylene (PTFE), which had been mechanically fractured in vacuo with tetracyanoethylene (TCNE) at 77 K. The assignment of \documentclass{article}\pagestyle{empty}\begin{document}${\rm TCNE}^{ \cdot ^ - } $\end{document} was carried out by ESR spectral simulation on the basis of an anisotropic effective hyperfine tensor that included a forbidden transition term. The \documentclass{article}\pagestyle{empty}\begin{document}${\rm TCNE}^{ \cdot ^ - } $\end{document} is formed by abstraction of an electron by TCNE from the anion that is produced by heterogeneous scission of the carbon-carbon bond in the main chain of PTFE. At least 16% of the scission of the main chains of PTFE occurs by a heterogeneous process to produce the anions. Approximately 50% of the anions decay during annealing for 30 min at 220 K in the dark, and all anions decay within 15 min at 325 K.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/polb.1987.090250706
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    Paper (German National Licenses)
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