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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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    Paper (German National Licenses)
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  • 2
    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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    Paper (German National Licenses)
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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
    Effects of bean and wheat α-amylase inhibitors on α-amylase activity and growth of stored product insect pests (1995)
    Springer
    Entomologia experimentalis et applicata 75 (1995), S. 237-244 
    Details
    ISSN: 1570-7458
    Keywords: amylase inhibitor ; red kidney bean ; hard red winter wheat ; growth ; insects ; beetles ; plant resistance ; stored products ; protease inhibitor
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Insect α-amylase inhibiting and/or growth inhibiting activities of proteinaceous inhibitors from red kidney bean (Phaseolus vulgaris) and hard red winter wheat (Triticum aestivum) were examined. The bean inhibitor was most effectivein vitro against α-amylases from the red flour beetle (Tribolium castaneum) and the confused flour beetle (T. confusum), followed by those from the rice weevil (Sitophilus oryzae) and yellow mealworm (Tenebrio molitor). The insect enzymes were from two- to 50-fold more susceptible than human salivary α-amylase. When the inhibitors were added at a 1% level to a wheat flour plus germ diet, the growth of red flour beetle larvae was slowed relative to that of the control group of larvae, with the bean inhibitor being more effective than the wheat inhibitor. Development of both the red flour beetle and flat grain beetle (Cryptolestes pusillus) was delayed by 1% bean inhibitor, but development of the sawtoothed grain beetle (Oryzaephilus surinamensis) and lesser grain borer (Rhyzopertha dominica) was not affected by either the bean or wheat inhibitor at the 1% level. Rice weevil adults fed a diet containing 1% bean or wheat inhibitor exhibited more mortality than weevils fed the control diet. When the wheat amylase inhibitor was combined with a cysteine protease inhibitor, E-64, and fed to red flour beetle larvae, a reduction in the growth rate and an increase in the time required for adult eclosion occurred relative to larvae fed either of the inhibitors separately. The bean inhibitor was just as effective alone as when it was combined with the protease inhibitor. These results demonstrate that plant inhibitors of insect digestive enzymes act as growth inhibitors of insects and possibly as plant defense proteins, and open the way to the use of the genes of these inhibitors for genetically improving the resistance of cereals to storage pests.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02382258
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  • 7
    Electronic Resource
    Electronic Resource
    Bruchid resistance of transgenic azuki bean expressing seed α-amylase inibitor of common bean (1996)
    Springer
    Entomologia experimentalis et applicata 79 (1996), S. 309-315 
    Details
    ISSN: 1570-7458
    Keywords: insect resistance ; genetic engineering ; host specificity ; transgenic plant ; α-amylase inhibitor ; Callosobruchus spp. ; Zabrotes subfasciatus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Various species of bruchid beetles including Callosobruchus chinensis, C. maculatus and C. analis cause postharvest damage of azuki bean seeds, an important East Asian grain legume. The α-amylase in the midguts of these insects is inhibited by the α-amylase inhibitor (αAI) present in common bean seeds. Transformation of azuki bean with the αAI gene driven by the promoter of phytohemagglutinin results in high levels of αAI in the seeds and the complete block of bruchid development on the seeds. Zabrotes subfasciatus, a South and Central American bruchid that is a storage pest of common bean, develops normally on the transgenic azuki bean.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00186289
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  • 8
    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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  • 9
    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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  • 10
    Electronic Resource
    Electronic Resource
    Incorporation of fucose into the carbohydrate moiety of phytohemagglutinin in developing Phaseolus vulgaris cotyledons (1983)
    Springer
    Planta 157 (1983), S. 454-461 
    Details
    ISSN: 1432-2048
    Keywords: Cotyledon ; Fucose ; Glycoprotein ; Phaseolus (hemagglutinin_ ; Phytohemagglutinin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Incubation of developing cotyledons of P. vulgaris with [3H]fucose resulted in the incorporation of radioactivity into the cell wall, membranous organelles and soluble macromolecules. Fractionation of the proteins by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, followed by fluorography, showed that phytohemagglutinin (PHA) was the major fucosylated protein synthesized in the cotyledons. Incorporation of fucose into PHA occurred in the membranous organelle fraction, and the radioactive fucose remained associated with the PHA during a 20-h chase of the radioactivity. Tunicamycin inhibited the incorporation of glucosamine and fucose into PHA to the same extent (65%), indicating the involvement of a lipid intermediate in the incorporation of fucose, or the attachment of fucose to the high-mannose oligosaccharide moiety of newly synthesized PHA. Digestion with proteinase K of [3H]fucose- or [3H]glucosamine-labeled PHA resulted in the formation of glycopeptides of similar size. These glycopeptides were partially resistant to digestion with endo-β-N-acetylglucosaminidase H, even after the removal of fucose by mild acid hydrolysis. We postulate, on the basis of these experiments, that the transport of PHA from the endoplasmic reticulum to the protein bodies is accompanied by the modification of its oligosaccharide side-chain. This modification involves inter alia the attachment of fucose, and renders the oligosaccharide side-chain resistant to digestion with endo-β-N-acetylglucosaminidase H. Analogy with animal glycoproteins indicates that this modification probably occurs in the Golgi apparatus.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00397203
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