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  • 1
    Electronic Resource
    Electronic Resource
    Further studies on the mechanism of inhibition of intestinal chylomicron transport by Pluronic L-81
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Lipids and Lipid Metabolism 1004 (1989), S. 357-362 
    Details
    ISSN: 0005-2760
    Keywords: Chylomicron formation ; Endoplasmic reticulum ; Golgi apparatus ; Intestinal lipoprotein ; VLDL
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/0005-2760(89)90084-2
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    The effect of cytochalasin B on the rate of growth and ultrastructure of wheat coleoptiles and maize roots (1979)
    Springer
    Planta 144 (1979), S. 373-383 
    Details
    ISSN: 1432-2048
    Keywords: Auxin ; Cell elongation ; Cytochalasin B ; Dictyosomes ; Secretion ; Triticum ; Zea
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Cytochalasin B (CB) inhibits the elongation growth of maize roots, and that of wheat coleoptile segments incubated in indolyl-3-acetic acid, by over 30% after a lag period of about 60 min. This long lag is not due to poor tissue penetration by the inhibitor, but seems to reflect a property of the process inhibited by CB. The only visible ultrastructural change accompanying growth inhibition is the accumulation of secretory vesicles in the vicinity of dictyosomes, which occurs between 90 and 300 min. However, a massive accumulation of vesicles is seen after 120 min in root cap cells which possess very active dictyosomes. The results indicate that CB does not inhibit elongation growth by interfering with cytoplasmic streaming. Instead, they indicate that the drug acts to inhibit the secretion of cell wall components at some stage after vesicle production, but prior to their transport.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00391581
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    The role of the epidermis in auxin-induced and fusicoccin-induced elongation of Pisum sativum stem segments (1980)
    Springer
    Planta 150 (1980), S. 371-379 
    Details
    ISSN: 1432-2048
    Keywords: Auxin ; Cell elongation ; Epidermis peeling ; Fusicoccin ; Pisum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The effects of peeling and wounding on the indole-3-acetic acid (IAA) and fusicoccin (FC) growth response of etiolated Pisum sativum L. cv. Alaska stem tissue were examined. Over a 5 h growth period, peeling was found to virtually eliminate the IAA response, but about 30% of the FC response remained. In contrast, unpeeled segments wounded with six vertical slits exhibited significant responses to both IAA and FC, indicating that peeling does not act by damaging the tissue. Microscopy showed that the epidermis was removed intact and that the underlying tissue was essentially undamaged. Neither the addition of 2% sucrose to the incubation medium nor the use of a range of IAA concentrations down to 10-8 M restored IAA-induced growth in peeled segments, suggesting that lack of osmotic solutes and supra-optimal uptake of IAA were not important factors over this time period. It is concluded that, although the possibility remains that peeling merely allows leakage of hydrogen ions into the medium, it seems more likely that peeling off the epidermis removes the auxin responsive tissue.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00390172
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Immunological detection and localization of a calsequestrin-like protein in red beet and cucumber cells (1994)
    Springer
    Protoplasma 179 (1994), S. 158-165 
    Details
    ISSN: 1615-6102
    Keywords: Beta vulgaris ; Calcium binding ; Calsequestrin ; Cucumis sativus ; Endoplasmic reticulum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Calsequestrin is a calcium binding protein present in the sarcoplasmic reticulum (SR) of animal muscle cells and is thought to be essential for the rapid uptake and release of Ca2+, and thus for the regulation of Ca2+-dependent cellular functions. Higher plant cells of red beet (Beta vulgaris L.) and cucumber (Cucumis sativus L.) contain a polypeptide of about Mr 55000 that cross-reacts with a monoclonal antibody raised against calsequestrin from rabbit skeletal muscle SR. In beet this protein changes its apparent molecular weight with pH as indicated in Western immunoblotting. Although this protein bound calcium it was not the dominant calcium-binding protein in red beet. Washing of beet root tissue leads to a slight increase of this polypeptide in microsomal fractions as indicated by immunoblotting. After immunoblotting to partially purified cell membrane fractions this polypeptide appeared to be predominantly associated with endoplasmic reticulum-enriched fractions. Immunogold labelling of ultrathin sections of cucumber hypocotyl using the anti-calsequestrin antibody showed that gold particles were very largely confined to the cytosol and often in close proximity to the ER. Clusters of up to nine gold particles were observed, often over small vesicular areas, as observed in some animal tissues. These results indicate that red beet and cucumber cells contain a protein which may be related to animal calsequestrin. It appears to be associated with the ER and could be involved in cellular calcium regulation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01403954
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    Paper (German National Licenses)
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