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  • ATPase cytochemistry  (2)
  • Endoplasmic reticulum  (2)
  • 1
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Lipids and Lipid Metabolism 1004 (1989), S. 357-362 
    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
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  • 2
    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
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Protoplasma 104 (1980), S. 55-65 
    ISSN: 1615-6102
    Keywords: ATPase cytochemistry ; Phloem ; Ricinus communis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Standard lead precipitation procedures have been used to examine the localization of ATPase activity in phloem tissues ofRicinus communis. Reaction product was localized on the plasma membrane of the companion cells associated with sieve elements and of parenchyma cells in phloem tissues from the leaf, petiole, stem and root. ATPase activity was also present on the plasma membrane and dispersed P-protein of sieve elements in petiole, stem and root tissue, but was absent from the plasma membrane of these cells in the leaf minor veins. Substitution ofβ-glycerophosphate for ATP produced no change in the localization of reaction product in leaf tissue. These findings are discussed in relation to current theories on the mechanism of sugar transport and phloem loading.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1615-6102
    Keywords: Analytical electron microscopy ; ATPase cytochemistry ; Plasma membrane ; Ricinus communis ; Triticum aestivum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The claim that osmium-containing deposits which lack lead are frequently and incorrectly interpreted as enzymatic reaction products in lead precipitation techniques for ATPase localization in plants is without foundation. Proper controls clearly demonstrate the enzymatic origin of membrane-located deposits and the presence of lead is confirmed by analytical electron microscopy.
    Type of Medium: Electronic Resource
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