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  • 1
    ISSN: 1432-2048
    Keywords: Key words:Brassica (germination) – Germination – Globulin breakdown –Phaseolus (germination) – Seedling growth –Vicia (germination)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract. The temporal and spatial patterns of storage-globulin mobilization were immunohistochemically pursued in the embryonic axis and cotyledons of vetch seed (Vicia sativa L.) during germination and early seedling growth. Embryonic axes as well as cotyledons of mature seeds contain protein bodies with stored globulins. Prevascular strands of axes and cotyledons, the radicle and epidermal layers of axis organs were nearly exclusively stained by vicilin antibodies whereas the cotyledonous storage mesophyll gave similar staining for vicilin and legumin. Globulin breakdown started locally where growth and differentiation commenced in the axis. There, vicilin mobilization preceded legumin mobilization. Thus vicilin represents the initial source of amino acids for early growth and differentiation processes in vetch. Legumin presumably only serves as a bulk amino acid source for subsequent seedling growth during postgerminative globulin degradation. During the first 2–3 d after the start of imbibition the axis was depleted of globulins whereas no decrease in immunostainability was detected in the cotyledons except in their vascular strands where immunostainability was almost completely lost at this time. Continuous vascular strands were established at the third day when globulin breakdown was finished in the axis but had just started in the cotyledon mesophyll. Protein mobilization proceeded in a small zone from the epidermis towards the vascular strands in the center of the cotyledons. In this zone the storage cells, which initially appeared densely packed with starch grains and protein bodies, concomitantly transformed into cells with a large central vacuole and only a thin cytoplasmic layer attached to the cell wall. These results agree well with the hypothesis that during the first 2 d after imbibition the axis is autonomous in amino acid provision. After the endogenous reserves of the axis are depleted and the conductive tissue has differentiated, globulins are mobilized in the cotyledons, suggesting that then the amino acid supply is taken over by the cotyledons. For comparison with other degradation patterns we used garden bean (Phaseolus vulgaris L) and rape (Brassica napus L.) as reference plants.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1573-5028
    Keywords: field bean (Vicia faba L.) ; seed ontogenesis ; a class of predominating mRNA ; cDNA sequence ; seed protein ; signal peptide processing
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract cDNA clones have been constructed bearing inserts for a specific mRNA class of high abundance in developing seeds of field bean (Vicia faba L.). Three full-length clones representing transcripts of different genes were sequenced and conceptually translated into a M=30 000 primary gene product. The structural analysis of the derived amino acid sequence revealed distinct domains: (i) a cleavable signal peptide; (ii) a hydrophilic N-terminal stretch possessing two serine clusters; (iii) a valine cluster and a hydrophobic domain in the C-terminal part of the polypeptide. The amino acid sequence of the polypeptide does not show homology with other known proteins. The corresponding mRNA could be isolated using cDNA clones and was efficiently translated in various systems. In a cell-free system the presence of a functional signal peptide was shown, which interacts with the signal recognition particle resulting in a cotranslational translocation across the membrane of the endoplasmic reticulum. If synthesized in Xenopus oocytes the translation product of the mRNA was secreted out of the cell. Homologous mRNA was found to be present also in developing cotyledons of pea (Pisum sativum L.) and french bean (Phaseolus vulgaris L.).
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Fresenius' Zeitschrift für analytische Chemie 23 (1884), S. 270-271 
    ISSN: 1618-2650
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Fresenius' Zeitschrift für analytische Chemie 22 (1883), S. 118-118 
    ISSN: 1618-2650
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Genetic resources and crop evolution 35 (1987), S. 25-52 
    ISSN: 1573-5109
    Source: Springer Online Journal Archives 1860-2000
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Description / Table of Contents: Summary The importance of protein yield, protein content, and protein quality of cereal grains and grain legumes increases as a factor of qualitative growth in agriculture. The extent of variability in protein characters represents a predominating basis for the breeding of new high yielding, protein rich and nutritionally improved varieties. Cereal and grain legume collections of the germplasm bank of the Gatersleben institute have been systematically screened with respect to specimens with outstanding protein characters. The variation in protein content of barley caryopses was extended by mutation induction, and the resulting mutants were used to investigate the general potentials for improving protein yield of barley by breeding varieties with increased grain protein content. Basic research was performed on the charakters of storage proteins, as well as on their biosynthesis and accumulation during legume seed development. The results explained several of the difficulties that arose in the breeding of protein-rich high-yielding varieties and in improving the nutritional quality of seed proteins, respectively. At present, the application of genetic engineering methods promises to open new possibilities of controlled amplification of nutritional characters of crop seed proteins. The review summarizes the contributions of the Zentralinstitut für Genetik und Kulturpflanzenforschung from 30 years of basic research on biochemistry and genetics of crop seed proteins, and discusses finally the perspectives for future solutions of the problems in breeding for high protein yield and improved grain protein quality, respectively.
    Abstract: Краткое содержание В сельскохозяйстве нном растениеводстве зерновых и зернобобовых культур такие факторы качественного роста как: сбор (сырого) белка на единицу площади, его содержание и качество, приобретают все более возрастающее значение. Культивирование новых высокоурожайных и богатых белком сортов, а также улучшение питательно-физиолог ического качества белков семян, исходит, прежде всего, из как можно более широкой амплитуды вариации белковых показателей у семян. Коллекции зерновых и зернобобовых культур генного банка гатерслебенского института были систематически исследованы в поисках форм с особо благоприятными значениями белковых показателей. С помощью индукций мутаций смогли расширить амплитуду вариации на содержание белка у ячменя и на ¶rt;том материале смоги проверить принципиальную возможность использования ¶rt;того признака для выведения новых высокоурожайных и богатых белком сортов. Фундаментальное исследование свойств запасных белков, их биозинтеза и аккумуляции во время развития семян способствовало решению ряда проблем, возникших при селекционном использовании, богатых белком или улучшенных по качеству белка, исходных форм. В настоящее время применение генной инженерии открывает новые пути для направленного расширения амплитулы вариации признаков качества белка. В предлагаемом обозрении обобщается вклад Центрального института генетики и исследования культурных растений в фундаментальные исследования в области биохимии и генетики белков семян на протяжении последних 30 лет и обсуждаются будущие перспективы для решения белковой проблемы в селекции зерновых и зернобобовых культур.
    Notes: Zusammenfassung Als Faktoren für ein qualitatives Wachstum im landwirtschaftlichen Pflanzenbau gewinnen Proteinertrag, Proteingehalt und Proteinqualität von Getreiden und Körnerleguminosen zunehmend an Bedeutung. Die Züchtung neuer ertrag- und proteinreicher Sorten sowie die Verbesserung der ernährungsphysiologischen Qualität von Samenproteinen geht vor allem von einer möglichst großen Variationsbreite in den Eiweißmerkmalen der Samen aus. Getreide- und Körnerleguminosen-Kollektionen der Genbank des Gaterslebener Institutes wurden systematisch nach Formen mit besonders günstigen Werten der Proteinmerkmale durchforscht. Mit Hilfe der Mutationsinduktion konnte die Variationsbreite im Proteingehalt bei Gersten ausgeweitet und an diesem Material die Aussicht auf Nutzung dieses Merkmals zur Züchtung neuer ertrag- und proteinreicher Sorten grundsätzlich geprüft werden. Grundlagenforschung über die Eigenschaften von Reserveproteinen, über ihre Biosynthese und Akkumulation während der Samenentwicklung ergab Erklärungen für eine Reihe von Problemen, die bei der züchterischen Nutzung proteinreicher oder in der Proteinqualität verbesserter Ausgangsformen auftreten. In neuester Zeit beginnt die Anwendung der Gentechnik neue Wege zur gezielten Erweiterung der Variationsbreite von Eiweißqualitätsmerkmalen zu eröffnen. In der vorliegenden Übersicht werden die Beiträge des Zentralinstitutes für Genetik und Kulturpflanzenforschung zur Grundlagenforschung auf dem Gebiet der Biochemie und Genetik von Samenproteinen aus einem Zeitraum von nunmehr 30 Jahren zusammengefaßt und die zukünftigen Aussichten zur Lösung der Proteinprobleme in der Getreide-und Körnerleguminationszüchtung diskutiert.
    Type of Medium: Electronic Resource
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  • 6
    ISSN: 1573-5028
    Keywords: cysteine proteinases ; differential gene expression ; enzyme families ; seed globulin proteolysis ; vacuolar localization ; Vicia sativa
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Families of papain- and legumain-like cysteine proteinases (CPR) were found in Vicia seeds. cDNAs and antibodies were used to follow organ specificity and the developmental course of CPR-specific mRNAs and polypeptides. Four papain-like cysteine proteinases (CPR1, CPR2, proteinase A and CPR4) from vetch seeds (Vicia sativa L.) were analysed. CPR2 and its mRNA were already found in dry embryonic axes. CPR1 was only detected there during early germination. Both CPR1 and CPR2 strongly increased later during germination. In cotyledons, both CPR1 and CPR2 were only observed one to two days later than in the axis. Proteinase A was not found in axes. In cotyledons it could only be detected several days after seeds had germinated. CPR4 mRNA and polypeptide were already present in embryonic axes and cotyledons during seed maturation and decreased in both organs during germination. Purified CPR1, CPR2 and proteinase A exhibited partially different patterns of globulin degradation products in vitro. Although the cDNA-deduced amino acid sequence of the precursor of proteinase A has an N-terminal signal peptide, the enzyme was not found in vacuoles whereas the other papain-like CPRs showed vacuolar localization. Four different legumain-like cysteine proteinases (VsPB2, proteinase B, VnPB1 and VnPB2) of Vicia species were analysed. Proteinase B and VnPB1 mRNAs were detected in cotyledons and seedling organs after seeds had germinated. Proteinase B degraded globulins isolated from mature vetch seeds in vitro. VsPB2 and proteinase B are localized to protein bodies of maturing seeds and seedlings, respectively, of V. sativa. Like VsPB2 from V. sativa, also VnPB2 of V. narbonensis corresponds to vacuolar processing enzymes (βVPE). Based on these results different functions in molecular maturation and mobilization of storage proteins could be attributed to the various members of the CPR families.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 6 (1986), S. 40-41 
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: DNA clones representing two subfamilies A and B of legum in genes and a recombinant phage containing a complete legumin B gene have been isolated and characterized by DNA sequencing. A DNA fragment harbouring the legumin B gene and adjacent sequences was used for Ti-mediated transfer into tobacco cells.
    Type of Medium: Electronic Resource
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