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  • 1
    Electronic Resource
    Electronic Resource
    Intracellular site of proline hydroxylation in plant cells (1971)
    s.l. : American Chemical Society
    Biochemistry 10 (1971), S. 4290-4294 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00799a021
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  • 2
    Electronic Resource
    Electronic Resource
    Preservation of the Ultrastructure of Plant Cells using Glutaric Acid Dialdehyde as a Fixative (1963)
    [s.l.] : Nature Publishing Group
    Nature 200 (1963), S. 711-712 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Carasso and Favard2 discuss in detail the chemical mode of action of formaldehyde as a fixative. Addition-reactions between formaldehyde and proteins and nucleic acids involve sulphydryl and amino-groups. The formation of methylene bridges between adjacent molecules can take place and aids in the ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/200711a0
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  • 3
    Electronic Resource
    Electronic Resource
    Inhibition of Gibberellic Acid Induced Formation of α-Amylase by Abscisin II (1966)
    [s.l.] : Nature Publishing Group
    Nature 212 (1966), S. 1066-1067 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Gibberellic acid is known to break dormancy in a number of higher plant systems, and so it has been proposed that the balance between dormancy and growth may be achieved by a balance of the levels of dormin (Ab II) and GA5. It is therefore of considerable interest to determine at what metabolic ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/2121066a0
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  • 4
    Electronic Resource
    Electronic Resource
    A precursor of the reserve-protein, phaseolin, is transiently associated with the endoplasmic reticulum of developing Phaseolus vulgaris cotyledons (1982)
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 55 (1982), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Developing cotyledons of Phaseolus vulgaris L. were labeled for 30 min with [3H] amino acids, homogenized, and the proteins fractionated on sodium dodecylsulfate (SDS) polyacrylamide gels. Fluorographs of these gels showed that the polypeptides of phaseolin, the major reserve protein of P. vulgaris, were synthesized as precursors which could be distinguished from the polypeptides of mature phaseolin by their slightly lower mobility.When extracts of cotyledons labeled for 45 min with [3H] amino acids were fractionated on isopynic sucrose gradients, radioactive phaseolin banded at the same density (1.14 g cm-3) as the endoplasmic reticulum (ER)-marker enzyme NADH-cytochrome c reductase. Fractionation in the presence of 3 mM MgCl2 indicated that the newly-synthesized phaseolin was associated with the rough ER. Pulse-chase experiments showed that phaseolin was transiently associated with the ER, and later accumulated in the protein bodies.Treatment of isolated ER with proteinase K showed that phaseolin polypeptides were degraded only if Triton X-100 was present, indicating that phaseolin was membrane-protected, probably enclosed within the vesicles. ER-associated phaseolin associated to an 18S form at pH 4.5 in the presence of 0.3 M NaCl and 100 mM sodium acetate. The polypeptides of ER-associated phaseolin had a slightly lower mobility on SDS-gels than polypeptides of protein body phaseolin. ER-associated phaseolin had a carbohydrate content of 6.8%, while protein body-derived phaseolin had a carbohydrate content of 6.2%. When cotyledons were labeled simultaneously with [14C] amino acids and [3H] glucosamine or with [14C] amino acids and [3H] mannose, the [3H]/[14C] ratio of ER-derived phaseolin was similar to that of protein body derived phaseolin, indicating that the faster mobility on SDS-gels was not due to the detachment of carbohydrate. Experiments in which the carbohydrate side chains were removed with endoglycosidase H, and the resulting polypeptides subjected to electrophoresis in SDS-gels showed that the differential mobility of the glycopolypeptides of phaseolin resided in their polypeptide chains.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1399-3054.1982.tb02268.x
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  • 5
    Electronic Resource
    Electronic Resource
    Structure, biosynthesis, and function of asparagine-linked glycans on plant glycoproteins (1989)
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 75 (1989), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: In plants, glycoproteins with asparagine-linked glycans (oligosaccharides) are found in vacuoles, in the extracellular space or matrix, and associated with the endo-membrane system (endoplasmic reticulum, Golgi apparatus, plasma membrane, tonoplast). These glycans are of the high-mannose type, with a structure identical to that found in other organisms (mammals, yeast), or of the complex type with a β1–2 linked xylosyl residue not found in mammalian complex glycans. Asparagine-linked glycans play multiple roles by modifying the physicochemical properties of the polypeptides to which they are attached.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1399-3054.1989.tb06187.x
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  • 6
    Electronic Resource
    Electronic Resource
    Transgenic Pea Seeds Expressing the α -Amylase Inhibitor of the Common Bean are Resistant to Bruchid Beetles (1994)
    [s.l.] : Nature Publishing Company
    Nature biotechnology 12 (1994), S. 793-796 
    Details
    ISSN: 1546-1696
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: [Auszug] Infestations of stored legume seeds by bruchid beetles, such as the cowpea weevil and the Azuki bean weevil cause substantial economic and nutritional losses of these food crops, especially in developing countries. Seeds of the common bean are resistant to these bruchids largely because of the ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/nbt0894-793
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  • 7
    Electronic Resource
    Electronic Resource
    Biosynthesis and release of cell wall-like glycoproteins during the vegetative cell cycle of Chlamydomonas reinhardii (1976)
    Springer
    Planta 129 (1976), S. 183-189 
    Details
    ISSN: 1432-2048
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The culture medium of asynchronously growing Chlamydomonas reinhardii cells contains distinct proteins which are derived from the cell walls of these cells. When cultures are synchronized by a light-dark cycle cell wall proteins are synthesized throughout the cycle, but the release of these proteins into the culture medium occurs primarily in the last quarter of the cycle, after cell separation has occurred. The mutant CW-2, which does not form a normal cell wall, continuously synthesizes and secretes cell wall proteins into the culture medium. The synthesis of cell wall protein during the cell cycle appears to be modulated and peaks of synthesis occur at the end of the light period and in the second half of the dark period, shortly after cell separation. At these times the cells devote 15% of their protein-synthetic capacity to making cell wall proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00390026
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  • 8
    Electronic Resource
    Electronic Resource
    Regulation of pentosan biosynthesis in barley aleurone tissue by gibberellic acid (1973)
    Springer
    Planta 111 (1973), S. 353-364 
    Details
    ISSN: 1432-2048
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Treatment of isolated barley aleurone layers with gibberellic acid (GA3) resulted in a progressive inhibition of cell-wall synthesis after a 4-h lag period. The incorporation of both [14C]arabinose and [14C]glucose into the cell wall was inhibited by GA3, but analysis of the labelled sugars in the polymerized product showed that the process most affected by the hormone treatment was pentosan biosynthesis. Labelling kinetics and pulse-chase analysis indicated that the pentosans were synthesized in the cytoplasm and subsequently transferred to the cell wall; GA3 did not significantly affect the latter step. The GA3-inhibited labelling of the cell-wall pentosans cannot be explained on the basis of an effect on uptake of radioactive cell-wall precursor, expansion of the free pentose pool, or degradation of newly-formed pentosan. GA3 inhibited the activity of a membrane-bound arabinosyl transferase present in the aleurone layers. This inhibition may explain the inhibition of cell-wall pentosan synthesis by GA3.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00385555
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  • 9
    Electronic Resource
    Electronic Resource
    Characterization and subcellular localization of vicilin and phytohemagglutinin, the two major reserve proteins of Phaseolus vulgaris L. (1978)
    Springer
    Planta 142 (1978), S. 291-298 
    Details
    ISSN: 1432-2048
    Keywords: Cotyledons ; Phaseolus ; Phytohemagglutinin ; Protein (reserve) ; Seeds (protein) ; Vicilin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Extracts of bean (Phaseolus vulgaris L. cv. Greensleeves) cotyledons contained two abundant proteins: vicilin and phytohemagglutinin. Vicilin, a 6.9 S protein fraction at neutral pH, associated to an 18.0 S form at pH 4.5 and had 3 non-identical subunits with molecular weights (MW) of 52,000, 49,000 and 46,000. Phytohemagglutinin, a 6.4 S protein fraction, had 2 non-identical subunits with MW of 34,000 and 36,000. Phytohemagglutinin could be separated by isoelectrofocusing into a mitogenic and non-erythroagglutinating protein with a single subunit of MW=34,000, and a mitogenic and erythroagglutinating protein fraction which contained both subunits. Vicilin is apparently identical with the so called glycoprotein II (A. Pusztai and W.B. Watt, Biochim. Biophys. Acta 365, 57–71, 1970) and with globulin G1 (R.C. McLeester, T.C. Hall, S.M. Sun, F.A. Bliss, Phytochem. 2, 85; 1973), while phytohemagglutinin is identical with globulin G2 (McLeester et al., 1973). Since vicilin and phytohemagglutinin are internationally used names there is no need to introduce new names to describe P. vulgaris reserve proteins. Both proteins are catabolized in the course of seedling growth and are located in the protein bodies, indicating that they are reserve proteins. Vicilin isolated in its 18.0 S form from the cotyledons of young seedlings contains substantial quantities of smaller polypeptides, in addition the 3 original ones. We suggest that the presence of these small polypeptides represents partial breakdown of the vicilin prior to its complete catabolism.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00385080
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  • 10
    Electronic Resource
    Electronic Resource
    The endoplasmic reticulum of mung-bean cotyledons (1980)
    Springer
    Planta 149 (1980), S. 361-369 
    Details
    ISSN: 1432-2048
    Keywords: Cotyledons ; Endoplasmic reticulum (biosynthesis) ; NADH-cytochrome-c reductase ; Vigna
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Germination and seedling growth of mungbean (Vigna radiata (L.) Wilczek) are accompanied by the incorporation of radioactive amino acids, glycerol, galactose, and glucosamine in an organelle fraction of the cotyledons which co-equilibrates with NADH-cytochrome-c-reductase activity at 1.13 g·cm−3 on isopycnic gradients containing 1 mM EDTA. Up to 20% of the newly synthesized proteins accumulate in this organelle fraction. The organelle fraction has been identified as rough endoplasmic reticulum (ER) on the basis of its increased density (1.16 g·cm−3) when 3 mM MgCl2 is included in all media. Seedling growth is also accompanied by a marked rise (more than 5-fold) in ER-associated NADH- and NADPH-cytochrome-c-reductase activity, and by the incorporation of59Fe into ER-associated heme. Other manifestations of the reorganization of the ER in the cotyledons include a relative increase in membrane-associated RNA (from 12% of total RNA after 12 h of imbibition to 23% after 6 d of growth), and a change in the pattern of polypeptides associated with the ER. These results provide further evidence for the extensive reorganization of the ER of the cotyledons which accompanies seedling growth. The reorganization includes the simultaneous breakdown of the pre-existing tubular ER and the biosynthesis of new ER components.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00571171
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