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  • 1
    Electronic Resource
    Electronic Resource
    Characterization of proteins and allergens in germinating castor seeds by immunochemical techniques (1976)
    s.l. : American Chemical Society
    Journal of agricultural and food chemistry 24 (1976), S. 103-107 
    Details
    ISSN: 1520-5118
    Source: ACS Legacy Archives
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/jf60203a029
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  • 2
    Electronic Resource
    Electronic Resource
    World-Wide Research, Immunochemical Study of Wheat, Barley, and Malt Proteins (1965)
    s.l. : American Chemical Society
    Journal of agricultural and food chemistry 13 (1965), S. 392-398 
    Details
    ISSN: 1520-5118
    Source: ACS Legacy Archives
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/jf60141a002
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  • 3
    Electronic Resource
    Electronic Resource
    Immunochemical characterization of protein in plant studies (1971)
    s.l. : American Chemical Society
    Journal of agricultural and food chemistry 19 (1971), S. 653-659 
    Details
    ISSN: 1520-5118
    Source: ACS Legacy Archives
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/jf60176a011
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  • 4
    Electronic Resource
    Electronic Resource
    Contribution of aleurone layer and scutellum to α-amylase synthesis and secretion in wheat and rice grains (1991)
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 82 (1991), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Intact aleurone layers from wheat (Triticum aestivum L. cv Camp Rémy) and rice (Oryza sativa L. cv Cigalon) grains both contained and secreted more α-amylase (EC 3.2.1.1.) than did the corresponding scutellar tissues. This discrimination was already evident at the earliest stages of germination at which the tissues could be isolated, and became more pronounced upon subsequent germination and growth. Isoenzyme patterns obtained upon isoelectric focusing showed a considerable polymorphism of the α-amylases of each cereal. The enzyme polymorphism pattern was the same in the aleurone layer and in the scutellum, but some secondary constituents appeared to be more specific for the one or the other of the tissues. Moreover, the isozymes found in the tissues were the same as those found to be secreted. A third α-amylase antigen which differs from the well established α1 and α11 forms was identified in the germinating wheat grains. The presence of Ca2+ in the secretion medium favoured maximum secretion of α-amylases from the wheat scutellum and aleurone layers, whereas it inhibited the secretion of the enzymes from the rice aleurone layer.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1399-3054.1991.tb00089.x
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  • 5
    Electronic Resource
    Electronic Resource
    La glutamate déshydrogénase au cours de la gamétogénèse mâle chez Medicago sativa (1985)
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 63 (1985), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Glutamate dehydrogenase during male gametogenesis in Medicago sativa.The multiple forms of the alfalfa (Medicago sativa L.) glutamate dehydrogenase (GDH; EC 1.4.1.2–4) are much more numerous in the pollen than in other organs, and in particular in the floral parts. The appearance of the pollen-specific GDH pattern during male gametogenesis has been followed using electrophoretic, cytological and immunochemical techniques. After the tetrad stage the uninucleate microspore has no glutamate dehydrogenase activity. This activity appears only in the mitochondria of the binucleate young pollen. At this stage the electrophoretic pattern displays a faint intensity, but is already identical to that of mature pollen. On the other hand, the use of monospecific antibodies has revealed the presence of antigen in the microspore, and in the young pollen there is as much antigen as in the mature pollen. Therefore the synthesis of GDH precedes its activation, which follows the first pollen mitosis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1399-3054.1985.tb01904.x
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  • 6
    Electronic Resource
    Electronic Resource
    Differential expression of two β-amylase genes of rye during seed development (1995)
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 94 (1995), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The expression of two β-amylase loci was analysed in the developing seeds of two inbred lines of rye (Secale cereale L.), one of which was a β-amylase deficient mutant. Enzymatic activity and the contents of enzymatic protein and mRNA specific for each of an endosperm-characteristic and ubiquitous β-amylase were determined throughout the course of caryopsis development. Both loci were expressed in the developing normal line caryopses according to different temporal and quantitative patterns. The ubiquitous enzyme-specific locus β-Amy 2 was expressed earlier; both mRNA and enzymatic protein accumulated to a maximum extent at 10 to 15 days after pollination. In contrast, the highest content of mRNA for endosperm β-amylase (encoded by the β-Amy I locus) was found 20 days after pollination, and the corresponding enzymatic protein accumulated throughout seed development. The expression of the β-Amy I locus was 30- to 40-fold higher than that of the β-Amy 2 locus in terms of maximum specific mRNA accumulation. The expression product of only the β-Amy 2 locus was found in the developing mutant line caryopses. The expression pattern of this locus was similar in the developing normal and mutant line seeds in terms of the temporal accumulation of mRNA and enzymatic protein. However, an approximately 4-fold higher level of ubiquitous β-amylase-specific mRNA was found in the mutant than in the normal line caryopses, and the content of ubiquitous β-amylase protein decreased to near zero at seed maturity in the mutant line, but not in the normal line, caryopses. The enzymatic activities of both β-amylases appeared to be regulated at the level of accumulated enzymatic protein.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1399-3054.1995.tb00778.x
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  • 7
    Electronic Resource
    Electronic Resource
    Immunohistochemical localization of β-amylase in resting barley seeds (1986)
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 67 (1986), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The cellular localization of β-amylase (EC 3.2.1.2) in resting barley seeds was investigated by immunohistochemistry. The monospecificity of the antibodies used was shown by immunoelectrophoresis and western blotting. An adaptation of the immunofluorescence technique allowed the localization of β-amylase. free of autofluorescence, in the different parts of the seed. In endosperm, there was β-amylase protein in aleurone layers, only in the starchy endosperm, where the distribution of the enzyme was not uniform. The β-amylase of starchy endosperm. which can be in a free or a hound form, was mainly localized around starch granules of different sizes. In the embryo. β-amylase was present only in the part of the scutellum in front of the first leaf. By immunoquantitation after separation of the seed parts, its was shown that the ratio between the amounts of enzyme in embryo and endosperm was less than 1/3000.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1399-3054.1986.tb05752.x
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  • 8
    Electronic Resource
    Electronic Resource
    Localization of Acetylcholinesterase by Immunofluorescence in Eel Electroplax (1970)
    [s.l.] : Nature Publishing Group
    Nature 225 (1970), S. 1149-1150 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Purified AChE, a gift of W. Leuzinger and D. Nach-mansohn (Columbia University), had been prepared following the method of Leuzinger and Baker3. The enzyme had a specific activity greater than 300 mmoles of acetylthiocholine/mg protein/h. A 1 mg solution, emulsified in Freund's complete adjuvant, ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/2251149a0
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  • 9
    Electronic Resource
    Electronic Resource
    Detection and partial characterization of two antigenically distinct β-amylases in developing kernels of wheat (1990)
    Springer
    Planta 181 (1990), S. 505-511 
    Details
    ISSN: 1432-2048
    Keywords: β-Amylase ; Pericarp ; Seed development ; Triticum (β-amylase)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A β-amylase (EC 3.2.1.2) was identified in the outer pericarp (βP) of developing seeds of wheat (Triticum aestivum L.) and compared with the well known β-amylase which is synthesized during seed development in the starchy endosperm (βE). The enzyme βP already exists in the tissues before anthesis and vanishes at the time when βE starts to accumulate. The isoelectric-focusing patterns of βP and βE are very similar. The relative molecular weight (Mr) of βP is slightly higher than that of βE (66 and 64.5 kDa, respectively). Both βP and βE exhibit common epitopes in addition to epitopes specific for each of them. The two enzymes were identified in small amounts in the green tissues of the developing seeds (inner pericarp and testa). No antigenic difference was detected between βP and the β-amylases of roots and leaves.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00193003
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  • 10
    Electronic Resource
    Electronic Resource
    Alpha-amylase inhibitor in cereals: Comparison of the protein in different rye, wheat and triticale seeds by using immunoblotting (1986)
    Weinheim : Wiley-Blackwell
    Electrophoresis 7 (1986), S. 176-179 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Several isoforms of the barley α-amylase inhibitor were detected in the purified protein fraction and seed extract after isoelectric focusing. Polymorphism not detected by protein staining was revealed by immunoblotting using an antiserum against barley α-amylase inhibitor. The antiserum, previously described as giving cross reactions with the inhibitors of rye and wheat, was used for comparing the electrophoretic patterns of the protein in several lines of rye, in several varieties of wheat and in different triticales. The antiserum was used for immunoblotting after isoelectric focusing at pH 3.5-10. The inhibitor was found in all samples but the degree of polymorphism was low. The same pattern was found for all lines of rye investigated. This pattern differed from the pattern found for wheat, but again, all cultivars of wheat investigated displayed similar patterns. Structural genes for the α-amylase inhibitors were identified in the A and R genomes. Identical genes may exist on the B and D genomes. The wheat and rye structural genes for α-amylase inhibitor were found to be expressed in the octoploid, hexaploid and tetraploid triticales.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150070406
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