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  • 1
    Monograph available for loan
    Monograph available for loan
    Philadelphia : Soc. for Industrial and Applied Mathematics
    Call number: M 93.1056
    Type of Medium: Monograph available for loan
    Pages: XI, 133 S.
    ISBN: 0898713099
    Uniform Title: Ondelettes
    Classification:
    C.1.6.
    Language: English
    Location: Upper compact magazine
    Branch Library: GFZ Library
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  • 2
    Call number: M 93.0936
    Type of Medium: Monograph available for loan
    Pages: xv, 785 S.
    ISBN: 2863321307
    Classification:
    C.1.8.
    Language: English
    Location: Upper compact magazine
    Branch Library: GFZ Library
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  • 3
    Monograph available for loan
    Monograph available for loan
    Cambridge : Cambridge Univ. Press
    Associated volumes
    Call number: M 94.0013 ; PIK Q 200-00-0142
    In: Cambridge studies in advanced mathematics
    Type of Medium: Monograph available for loan
    Pages: XV, 223 S.
    ISBN: 0521420008
    Series Statement: Cambridge studies in advanced mathematics 37
    Classification:
    C.1.6.
    Language: English
    Location: Upper compact magazine
    Location: A 18 - must be ordered
    Branch Library: GFZ Library
    Branch Library: PIK Library
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  • 4
    Unknown
    Amsterdam ; New York : North-Holland
    Pages: Online-Ressource (x, 274 pages)
    ISBN: 9780444103574
    Language: English
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  • 5
    ISSN: 1432-1432
    Keywords: Key words: Gene families — Glutamine synthetase —Medicago truncatula— Phylogeny
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract. Glutamine synthetase type I (GSI) genes have previously been described only in prokaryotes except that the fungus Emericella nidulans contains a gene (fluG) which encodes a protein with a large N-terminal domain linked to a C-terminal GSI-like domain. Eukaryotes generally contain the type II (GSII) genes which have been shown to occur also in some prokaryotes. The question of whether GSI and GSII genes are orthologues or paralogues remains a point of controversy. In this article we show that GSI-like genes are widespread in higher plants and have characterized one of the genes from the legume Medicago truncatula. This gene is part of a small gene family and is expressed in many organs of the plant. It encodes a protein similar in size and with between 36 and 46% amino acid sequence similarity to prokaryotic GS proteins used in the analyses, whereas it is larger and with less than 25% similarity to GSII proteins, including those from the same plant species. Phylogenetic analyses suggest that this protein is most similar to putative proteins encoded by expressed sequence tags of other higher plant species (including dicots and a monocot) and forms a cluster with FluG as the most divergent of the GSI sequences. The discovery of GSI-like genes in higher plants supports the paralogous evolution of GSI and GSII genes, which has implications for the use of GS in molecular studies on evolution.
    Type of Medium: Electronic Resource
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  • 6
    ISSN: 1432-1432
    Keywords: Key words: Thioredoxins — Introns — Phylogeny
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract. In contrast to prokaryotes, which typically possess one thioredoxin gene per genome, three different thioredoxin types have been described in higher plants. All are encoded by nuclear genes, but thioredoxins m and f are chloroplastic while thioredoxins h have no transit peptide and are probably cytoplasmic. We have cloned and sequenced Arabidopsis thaliana genomic fragments encoding the five previously described thioredoxins h, as well as a sixth gene encoding a new thioredoxin h. In spite of the high divergence of the sequences, five of them possess two introns at positions identical to the previously sequenced tobacco thioredoxin h gene, while a single one has only the first intron. The recently published sequence of Chlamydomonas thioredoxin h shows three introns, two at the same positions as in higher plants. This strongly suggests a common origin for all cytoplasmic thioredoxins of plants and green algae. In addition, we have cloned and sequenced pea DNA genomic fragments encoding thioredoxins m and f. The thioredoxin m sequence shows only one intron between the regions encoding the transit peptide and the mature protein, supporting the prokaryotic origin of this sequence and suggesting that its association with the transit peptide has been facilitated by exon shuffling. In contrast, the thioredoxin f sequence shows two introns, one at the same position as an intron in various plant and animal thioredoxins and the second at the same position as an intron in thioredoxin domains of disulfide isomerases. This strongly supports the hypothesis of a eukaryotic origin for chloroplastic thioredoxin f.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Copenhagen : Munksgaard International Publishers
    Physiologia plantarum 103 (1998), S. 0 
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Flax (Linum usitatissimum) hypocotyl protoplasts immobilized in a calcium-alginate matrix give rise to embryo-like structures. A direct correlation was established between the presence of a set of ionically-bound cell wall proteins, which includes the basic polypeptides P184 and P183 with an apparent molecular mass of 25 kDa, and this morphogenic response. Microsequencing of tryptic fragments from P184 and P183 indicated homologies with the chitinase family. These homologies were confirmed by demonstrating that, after renaturation, such proteins express a potential chitinase activity in SDS-PAGE gel containing glycol chitin as synthetic substrate. Using degenerate primers from P184 internal sequences, we isolated one partial genomic sequence of a chitinase of 626 bp from which a putative 74-amino acid sequence, disrupted by one intron, was deduced. High degrees of homology with several plant chitinases, including those expressed during somatic embryogenesis or in seeds, were observed. P184 microsequences match the corresponding sequence deduced from the chitinase PCR-fragment perfectly.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Springer
    Journal of mathematical sciences 26 (1984), S. 2247-2248 
    ISSN: 1573-8795
    Source: Springer Online Journal Archives 1860-2000
    Topics: Mathematics
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Springer
    Protoplasma 81 (1974), S. 363-372 
    ISSN: 1615-6102
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary A new method is proposed for the isolation of tobacco mesophyll protoplasts in which salts were used as the plasmolyticum instead of the traditionally applied sugars. With this method protoplasts were regularly obtained and practically independent of the physiological state of the plants. In addition, a salt medium was developed in which the majority of protoplasts dedifferenciate and divide at a developmental state in which no wall could be detected by plasmolysis. After transferring these cells into another medium they were able to regenerate a wall and to divide.
    Type of Medium: Electronic Resource
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  • 10
    ISSN: 1432-2048
    Keywords: Cell wall formation ; Cytokinesis ; Inhibitors ; Mitosis ; Nicotiana
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The effect of cytochalasin B, colchicine, coumarin and 2,6-dichlorobenzonitrile on cell wall formation and cellular division was studied by light and electron microscopy with tobacco mesophyll protoplasts cultivated in vitro. 2,6-dichlorobenzonitrile was found to be the most effective and reversible inhibitor of cell wall formation. The other inhibitors caused irreversible damage and/or inhibited mitosis. In protoplasts cultivated in the presence of 2,6-dichlorobenzonitrile the total inhibition of cell wall formation had no effect on nuclear division, but cytokinesis was totally inhibited so that multinucleate protoplasts were obtained.
    Type of Medium: Electronic Resource
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