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  • 1
    Electronic Resource
    Electronic Resource
    Localization of ATPase in the endoplasmic reticulum and golgi apparatus of barley aleurone (1987)
    Springer
    Protoplasma 138 (1987), S. 73-88 
    Details
    ISSN: 1615-6102
    Keywords: ATPase ; Barley aleurone ; Endoplasmic reticulum ; Gibberellic acid ; Golgi apparatus ; Secretion
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The cytochemical localization of adenosine triphosphatase (ATPase) was studied in the aleurone layer of barley (Hordeum vulgare L. cv. Himalaya). Isolated barley aleurone layers secrete numerous enzymes having acid phosphatase activity, including ATPase. The secretion of these enzymes was stimulated by incubation of the aleurone layer in gibberellic acid (GA3). ATPase was localized using the metal-salt method in tissue incubated in CaCl2 with and without GA3. In sections of tissue incubated without GA3, cytochemical staining was confined to a narrow band of cytoplasm adjacent to the starchy endosperm and to the cell wall of the innermost tier of aleurone cells. Cytochemical staining was absent from the organelles of tissues not treated with GA3. In tissue incubated in the presence of GA3, cytochemical staining was evident throughout the cytoplasm and cell walls of the tissue. In the cell wall, electron-dense deposits were found only in digested channels. The cell-wall matrix of GA3-treated aleurone did not stain, indicating that it does not permit diffusion of enzyme. In the cytoplasm of GA3-treated aleurone, all organelles except microbodies, plastids, and spherosomes stained for ATPase activity; endoplasmic reticulum (ER), Golgi apparatus, and mitochondria showed intense deposits of stain. The ER of the aleurone is a complex system made up of flattened sheets of membrane, which may be associated with both the Golgi apparatus and the plasma membrane. The dictyosome did not stain uniformly for ATPase activity; rather there was a gradation in staining of the cisternae from thecis (lightly stained) to thetrans (heavily stained) face. Vesicles associated with dictyosome cisternae also stained intensely as did the protein bodies of GA3-treated aleurone cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01281016
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Localization of α-amylase isozymes within the endomembrane system of barley aleurone (1990)
    Springer
    Protoplasma 154 (1990), S. 16-24 
    Details
    ISSN: 1615-6102
    Keywords: α-Amylase isozymes ; Barley aleurone ; Endoplasmic reticulum ; Golgi apparatus ; Immunocytochemistry ; Intracellular transport
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The localization of α-amylase (EC 3.2.1.1) in barley (Hordeum vulgare L. cv Himalaya) aleurone protoplasts was studied using electron microscope immunocytochemistry. Antibodies were raised against total barley α-amylase, i.e., α-amylase containing both highisoelectric point (high-pI) and low-pI isoforms, as well as against purified high- and low-pI isoforms. All antibodies localized α-amylase to the endoplasmic reticulum (ER) and Golgi apparatus (GApp) of the aleurone cell, and various controls showed that the labeling was specific for α-amylase. Labeling of protein bodies and spherosomes, which are the most abundant organelles in this cell, was very low. There was no evidence that α-amylase isoforms were differentially distributed within different compartments of the endomembrane system. Rather, both high- and low-pI isoforms showed the same pattern of distribution in ER and in the cis, medial, and transregions of the GApp. We conclude that in the Himalaya cultivar of barley, all isoforms of α-amylase are transported to the plasma membrane via the GApp.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01349531
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Estimating viability of plant protoplasts using double and single staining (1986)
    Springer
    Protoplasma 135 (1986), S. 80-87 
    Details
    ISSN: 1615-6102
    Keywords: Barley aleurone ; Fluorescein diacetate ; Propidium iodide ; Protoplasts ; Viability determination ; Vital stains
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The utility of numerous dyes for determining the viability of barley (Hordeum vulgare L. cv. Himalaya) aleurone protoplasts was studied. Protoplasts isolated from the barley aleurone layer synthesize and secrete α-amylase isozymes in response to treatment with gibberellic acid (GA) and Ca2+. These cells also undergo dramatic morphological changes which eventually result in cell death. To monitor the viability of protoplasts during incubation in GA and Ca2+, several types of fluorescent and nonfluorescent dyes were tested. Evans blue and methylene blue were selected as nonfluorescent dyes. Living cells exclude Evans blue, but dead cells and cell debris stain blue. Both living and dead cells take up methylene blue, but living cells reduce the dye to its colorless form whereas dead cells and cell debris stain blue. The relatively low extinction coefficient of these dyes sometimes makes it difficult to distinguish blue-stained cells against a background of blue dye. Several types of fluorescent dyes were tested for their ability to differentially stain dead or living cells. Tinopal CBS-X, for example, stains only dead cells, and its high extinction coefficient allows its ultraviolet fluorescence to be recorded even when preparations are simultaneously illuminated with visible light. To double-stain protoplasts, the most effective stain was a combination of fluorescein diacetate (FDA) and propidium iodide (PI). By employing a double-exposure method to record the fluorescence from cells stained with both FDA and PI, dead and living cells could be distinguished on the basis of fluorochromasia.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01277001
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    Paper (German National Licenses)
    Fulltext
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