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  • 1
    Electronic Resource
    Electronic Resource
    Regulation of Ribonucleic Acid Metabolism by Plant Hormones (1977)
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Plant Physiology 28 (1977), S. 537-564 
    Details
    ISSN: 0066-4294
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1146/annurev.pp.28.060177.002541
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  • 2
    Electronic Resource
    Electronic Resource
    Gibberellic acid enhances the level of translatable mRNA for α-amylase in barley aleurone layers (1976)
    [s.l.] : Nature Publishing Group
    Nature 260 (1976), S. 166-169 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] In an attempt to relate GA3-stimulated a-amylase production to the level of ?-amylase mRNA, we have assayed for this mRNA by translating total and poly(A)-containing RNA isolated from aleurone layers in a cell-free system derived from wheat embryos21. This was followed by im-munoprecipitation22 and ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/260166a0
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  • 3
    Electronic Resource
    Electronic Resource
    Control of transcription of α -amylase and rRNA genes in barley aleurone protoplasts by gibberellin and abscisic acid (1985)
    [s.l.] : Nature Publishing Group
    Nature 316 (1985), S. 275-277 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Nuclei were isolated from GA3-responsive aleurone cell protoplasts16 and to facilitate this, several minor changes were made to our earlier protoplast preparation procedure. Figure 1 shows that, using the modified procedure, very little a-amylase activity accumulated in control protoplasts, that ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/316275a0
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  • 4
    Electronic Resource
    Electronic Resource
    The structure and composition of aleurone grains in the barley aleurone layer (1971)
    Springer
    Planta 101 (1971), S. 189-209 
    Details
    ISSN: 1432-2048
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Cytochemical methods have been used in conjunction with light and electron microscopy to determine the nature of the inclusions in aleurone grains of barley aleurone layers. Two kinds of inclusions were found: (1) Globoids within globoid cavities which were not enclosed by a membrane: the globoids stained red with toluidin blue due to the presence of phytin, and with lipid stains; (2) Protein-carbohydrate bodies which stained green with toluidin blue. The characteristics of globoids and protein-carbohydrate bodies as seen in the electron microscope are described in detail using both glutaraldehyde- and permanganatefixed tissues. The protein-carbohydrate body was identified by silver-hexaminestaining; this was not caused by carbohydrate but by some component which stained green in toluidin blue and which also occurred in cell walls in a thin band adjacent to the cytoplasm. The characteristics of both bodies are discussed in relation to apparent confusion in their identities in previous electron-microscope studies.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00386828
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  • 5
    Electronic Resource
    Electronic Resource
    Amylolytic activity in germinated Agrostemma githago L. seeds (1986)
    Springer
    Planta 168 (1986), S. 77-83 
    Details
    ISSN: 1432-2048
    Keywords: Agrostemma ; α-Amylase ; Perisperm ; Seed germination ; Starch reserves (degradation)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The perisperm of seeds of Agrostemma githago contains starch reserves which constitute 40% of the dry weight of the mature seed. These starch reserves were mostly broken down between 48 and 96 h after initiation of imbibition. (Germination occurred after 24 h.) The mode of starch degradation showed close parallels with the breakdown of the starchy endosperm in cereals. Thus, between 24 and 96 h the cotyledons secreted α-amylase (EC 3.2.1.1) whereas other degradative enzymes in the perisperm, β-amylase (EC 3.2.1.2) and maltase (EC 3.2.1.20), appeared to originate in the perisperm itself. Cotyledons secreted similar levels of α-amylase in the presence and absence of exogenous starch, indicating that secretion is an internal developmental event of the embryo. By isoelectric focussing the secreted α-amylase was separated into two isoenzymes. In the cotyledons, several other starch-degrading isoenzymes were present but were not secreted.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00407012
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  • 6
    Electronic Resource
    Electronic Resource
    The structure and composition of Aleurone grains in the Barley Aleurone layer (1971)
    Springer
    Planta 101 (1971), S. i 
    Details
    ISSN: 1432-2048
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00386827
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    Paper (German National Licenses)
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  • 7
    Electronic Resource
    Electronic Resource
    Gibberellic-acid-responsive protoplasts from mature aleurone of Himalaya barley (1985)
    Springer
    Planta 163 (1985), S. 430-438 
    Details
    ISSN: 1432-2048
    Keywords: Aleurone protoplasts ; α-Amylase ; Anaerobiosis ; Barley ; Gibberellin Hordeum (aleurone) ; Protoplast (aleurone)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Gibberellic acid (GA3)-responsive protoplasts were prepared from mature aleurone layers of Himalaya barley. Protoplasts prepared in air (air-protoplasts) synthesized α-amylase (EC 3.2.1.1) in the presence of GA3 at a rate which was 4–5 times greater that in its absence. Protoplasts prepared in nitrogen (N2-protoplasts) took longer than air-protoplasts to respond to GA3 but α-amylase synthesis ultimately attained a rate which was similar to that for air-protoplasts and which was many times that occurring in the absence of the hormone. Many characteristics of the protoplast response were similar to those of intact aleurone layers. α-Amylase arose by new synthesis, its synthesis was inhibited by abscisic acid, it was isozymically similar to aleurone layer enzyme, most of it was secreted into the incubation medium and its synthesis was accompanied by accumulation of α-amylase mRNA. GA3-induced changes in protein synthesis and cell structure also resembled those of intact aleurone cells. We conclude that the response of the protoplasts to GA3 is normal and that they present a useful system for the study of GA3 action in barley aleurone.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00395154
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  • 8
    Electronic Resource
    Electronic Resource
    Localization of gibberellic acid-induced acid phosphatase activity in the endoplasmic reticulum of barley aleurone cells with the electron microscope (1979)
    Springer
    Planta 147 (1979), S. 134-140 
    Details
    ISSN: 1432-2048
    Keywords: Aleurone ; Hordeum ; Endoplasmic reticulum ; Enzyme localization ; Phosphatase (acid)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A metal-salt precipitation method with p-nitrophenyl phosphate as substrate has been used to localize in the electron microscope acid phosphatase activity in isolated aleurone layers of barley (Hordeum vulgare L.), treated for 16 h in the presence or absence of gibberellic acid (GA3). The paper confirms results obtained earlier with an azo-dye precipitation method of enzyme localization. In addition the results show for the first time that in GA3-treated tissue enzyme activity is associated with the endoplasmic reticulum (ER), there being reaction product deposited in the ER cisternae. It is suggested that this activity represents new enzyme synthesized on ER in response to GA3 and probably destined for secretion.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00389513
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  • 9
    Electronic Resource
    Electronic Resource
    A structural study of germination in celery (Apium graveolens L.) seed with emphasis on endosperm breakdown (1979)
    Springer
    Planta 144 (1979), S. 241-248 
    Details
    ISSN: 1432-2048
    Keywords: Apium ; Endosperm breakdown ; Germination (seeds)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Germination of celery seed occurred after 6 d of imbibition in light. During this time the embryo enlarged at the expense of the adjacent endosperm cells and at the time of germination was 2–3 times as long as in the dry seed. Breakdown of the endosperm cells near the root cap preceeded radicle emergence. None of these changes occurred in darkness. Endosperm digestion began adjacent to the embryo and spread radially. In degrading cells, the aleurone grains often became larger and fewer in number. The cell walls were modified and appeared to undergo partial degradation. Ultimately the cells seemed to lose their contents. In cells adjacent to the root cap, similar changes occurred except there was a transient appearance of starch grains. Radial progression of endosperm breakdown also occurred in isolated endosperm treated with gibberellin A4+7. The results indicate that (1) the stimulus for breakdown of celery endosperm emanates from the embryo in response to light; (2) the stimulus may be a gibberellin because changes in endosperm cells and the sequence of endosperm digestion during germination resemble the responses of isolated endosperm to gibberellin; and (3) the radial progression of endosperm breakdown during germination may be the result of a sequential response of cells to a uniformly applied stimulus rather than the result of gradual embryo expansion.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00388765
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  • 10
    Electronic Resource
    Electronic Resource
    Cytochemical localization of phosphatase in barley aleurone cells: The pathway of gibberellic-acid-induced enzyme release (1974)
    Springer
    Planta 120 (1974), S. 81-105 
    Details
    ISSN: 1432-2048
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Acid phosphatase has been localized by cytochemical techniques in aleurone layers of dry barley (Hordeum vulgare L.) grains, in imbibed half-grains and in isolated layers treated with and without gibberellic acid (GA3). A major fraction of the enzyme activity is located in the cell walls. During imbibition and incubation of layers without GA3 a steady increase of enzyme activity in the inner wall region indicates a continued release of enzyme into the walls, but there is no essential change in the distribution of wall-enzyme sites. On the other hand, when GA3 is present enzyme activity is found for the first time in regions of the wall that become digested during GA3 treatment. These results indicate that the digested wall channels act as preferential routes through which acid phosphatase is released from the aleurone layer. No digested wall channels are formed in the absence of GA3 and, there being no route for release of the enzyme, it accumulates in the inner regions of the wall around aleurone cells. Assays of enzyme activity in vitro support the conclusions based on the histochemical data. They indicate that release of acid phosphatase from aleurone layers is under strict GA3 control, but that some of the increase in acid phosphatase activity in the isolated during incubation is not GA3 dependent. Acid phosphatase is present in the protein matrix of aleurone grains in all stages except the dry grain. Enzyme activity persists in aleurone grains throughout GA3 treatment when enlargement of the grains and mobilization of reserves takes place. It is suggested that this phosphatase hydrolyses phosphate reserves within the aleurone grains.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00388273
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