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  • 1
    Series available for loan
    Series available for loan
    Berlin : Selbstverl. Fachbereich Geowissenschaften
    Associated volumes
    Call number: SR 90.0061(115)
    In: Berliner geowissenschaftliche Abhandlungen
    Type of Medium: Series available for loan
    Pages: 123 S.
    ISBN: 3927541117
    Series Statement: Berliner geowissenschaftliche Abhandlungen : Reihe A, Geologie und Paläontologie 115
    Language: German
    Location: Lower compact magazine
    Branch Library: GFZ Library
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Munksgaard International Publishers
    Physiologia plantarum 118 (2003), S. 0 
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Plant cells require a co-ordination of metabolism between their major compartments, the plastids and the cytosol, in particular as certain metabolic pathways are confined to either compartments. The inner envelope membrane of the plastids forms the major barrier for metabolite exchange and is the site for numerous transport proteins, which selectively catalyse metabolite exchanges characteristic for green and/or non-green tissues. This report is focused on the molecular biology, evolution and physiological function of the family of phosphate translocators (PT) from plastids. Until now, four distinct subfamilies have been identified and characterized, which all share inorganic phosphate as common substrate, but have different spectra of counter exchange substrates to fulfil the metabolic needs of individual cells and tissues. The PTs are named after their main transported substrate, triose phosphate (TPT), phosphoenolpyruvate (PPT), glucose 6-phosphate (GPT) and xylulose 5-P (XPT). All PTs belong to the TPT/nucleotide sugar transporter (NST) superfamily, which includes yet uncharacterized PT homologues from plants and other eukaryotes. Transgenic plants or mutants with altered transport activity of some of the PTs have been generated or isolated. The analysis of these plant lines revealed new insights in the co-ordination and flexibility of plant metabolism.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1432-2048
    Keywords: Key words: Antisense repression/overexpression – Car-bohydrate metabolism – Carbon partitioning –Flaveria– Nicotiana (transgenic) – Triose phosphate/phosphate translocator – Starch mobilisation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract.  The physiological properties of transgenic tobacco plants (Nicotiana tabacum L.) with decreased or increased transport capacities of the chloroplast triose phosphate/phosphate translocator (TPT) were compared in order to investigate the extent to which the TPT controls metabolic fluxes in wild-type tobacco. For this purpose, tobacco lines with an antisense repression of the endogenous TPT (αTPT) and tobacco lines overexpressing the TPT gene isolated from the C4 plant Flaveria trinervia (FtTPT) were used. The F. trinervia TPT expressed in yeast cells exhibited transport characteristics identical to the TPT from C3 plants. Neither antisense TPT plants nor FtTPT overexpressors showed a phenotype when grown in a greenhouse in air. Contents of starch and soluble sugars in upper source leaves were similar in TPT underexpressors and FtTPT overexpressors compared to the wild type at the end of the photoperiod. The FtTPT overexpressors incorporated more 14CO2 in sucrose than the wild type, indicating that the TPT limits sucrose biosynthesis in the wild type. There were only small effects on labelling of amino acids and organic acids. The mobilisation of starch was enhanced in αTPT lines but decreased in FtTPT overexpressors compared to the wild type. Enzymes involved in starch mobilisation or utilisation, such as α-amylase or hexokinase were increased in αTPT plants and, in the case of amylases, decreased in FtTPT overexpressors. Moreover, α-amylase activity exhibited a pronounced diurnal variation in αTPT lines with a maximum activity after 8 h in the light. These changes in starch hydrolytic activities were confirmed by activity staining of native gels. Activities of glucan phosphorylases were unaffected by either a decrease or an increase in TPT activity. There were also effects of TPT activities on steady-state levels of phosphorylated intermediates as well as total amino acids and malate. In air, there was no or little effect of altered TPT transport activity on either rates of photosynthetic electron transport and/or CO2 assimilation. However, in elevated CO2 (1500 μl · l−1) and low O2 (2%) the rate of CO2 assimilation was decreased in the αTPT lines and was slightly higher in FtTPT lines. This shows that the TPT limits maximum rates of photosynthesis in the wild type.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1432-2048
    Keywords: Amphiphilic α-helix ; cDNA sequence ; Chloroplast protein import ; Phosphate translocator Pisum (phosphate translocator) ; Spinacia (phosphate translocation) ; Transit peptide
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Using an 5′-AvaII fragment of the spinach (Spinacia oleracea L.) phosphate translocator cDNA as a probe for a hybridization screening of a pea (Pisum sativum L.) cDNA library we have cloned and sequenced a cDNA clone coding for the phosphate translocator precursor protein from pea chloroplasts. The full-length cDNA clone comprises 42 base pairs (bp) at the 5′-non-coding region, a 1206-bp coding region corresponding to a polypeptide of 402 amino-acid residues (relative molecular mass 43 671) and 244 bp at the non-coding 3′-region. Determination of the N-terminal sequence of the phosphate translocator from both pea and spinach chloroplasts revealed that the transit peptides consist of 72 and 80 amino-acid residues, respectively. These transit peptides are different from those of other chloroplastic transit peptides in that they both contain an amphiphilic α-helix which is located either in close proximity to the processing site in pea or at the N-terminus in spinach. The mature proteins from pea and spinach both contain about 87% identical amino-acid residues and about seven putative membrane-spanning α-helices. Some of these α-helices have an amphiphilic character and might serve to form a hydrophilic translocation channel through the membrane. The in-vitro synthesized pea precursor protein is directed to the chloroplast and inserted into the chloroplast envelope membrane.
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 1546-170X
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] Protective immunity against Mycobacterium tuberculosis involves major histocompatibility complex class I (MHC-I)- and CD1-restricted CD8 T cells, but the mechanisms underlying antigen delivery to antigen-presenting molecules remain enigmatic. Macrophages, the primary host cells for mycobacteria, ...
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  • 6
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Polypeptide profiles of envelope membranes from spinach and pea chloroplasts are shown in Fig. la. The main poly-peptides of these membranes have different apparent relative molecular masses (Mr) of 29,000 (29 K; E29 (spinach); lane 1), and 30K (E30 (pea); lane 2). When the precursor proteins are ...
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  • 7
    ISSN: 1573-5028
    Keywords: Spinacia oleracea ; chemical cleavage ; gene expression ; polymerase chain reaction ; protein transport ; SDS-PAGE
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The 24 kDa outer envelope membrane protein of spinach chloroplasts (omp24) represents a major constituent of this membrane. Sequences of tryptic and endoprotease Glu-C peptides derived from omp24 allowed the design of oligonucleotides which were used to generate a DNA fragment by polymerase chain reaction using spinach cDNA as template. This fragment served as a probe to screen a cDNA library for a full-length clone of the omp24 coding sequence. The protein predicted from the complete sequence only has 148 amino acids and a molecular mass of 16294 Da. It is an acidic protein (calculated isoelectric point 4.8) with a high content of proline residues. Expression of the coding sequence in Escherichia coli and characterization of the purified recombinant protein produced revealed that the overestimation of its molecular mass by SDS-PAGE (ca. 25 kDa) is due to its abnormal amino acid composition. Despite its rather low hydrophobicity (polarity index 49%), omp24 appears to be deeply embedded in the outer membrane. Insertion of omp24 into the membrane proceeds almost independently of surface receptors or targeting sequence but, in contrast to other known outer envelope membrane proteins, is stimulated by ATP.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Chichester [u.a.] : Wiley-Blackwell
    International Journal for Numerical Methods in Engineering 12 (1978), S. 931-940 
    ISSN: 0029-5981
    Keywords: Engineering ; Engineering General
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Mathematics , Technology
    Notes: A new method for numerically solving the convection equation is presented. The reduction of numerical errors is achieved by introducing an auxiliary variable and solving an auxiliary equation for the latter. The method is based on a Hermite interpolation of the convected quantity. Three explicit numerical versions of the method are investigated and compared with some of the most widely used schemes, and it is shown that the new method gives better physical results. Arguments are given that the usual mathematical series expansions do not work sufficiently well in that context. Instead of using linear stability analyses the quality of the method is investigated by numerical experiments.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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  • 9
    Publication Date: 2016-08-31
    Description: Hydrogenation of liquid organic hydrogen carriers (LOHC) is usually carried out in liquid phase. To measure the kinetic of this hydrogenation an experimental setup using insitu Raman-spectroscopy for analysis of the reaction mixture is proposed. With this setup it is possible to perform hydrogenation reaction at temperatures of up to 573 K and pressures up to 25 MPa. For validation of the experimental setup the hydrogenation of 1octene was measured in liquid phase. It is shown that the reaction progress can be monitored in detail by Ramanspectroscopy. To determine kinetic parameters from the experimental data two modeling approaches were used: a classic kinetic model (CKM) and a thermodynamic kinetic model (TKM). These results were compared to literature data.
    Print ISSN: 0930-7516
    Electronic ISSN: 1521-4125
    Topics: Chemistry and Pharmacology , Process Engineering, Biotechnology, Nutrition Technology
    Published by Wiley
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  • 10
    Publication Date: 2017-10-01
    Print ISSN: 2055-026X
    Electronic ISSN: 2055-0278
    Topics: Biology
    Published by Springer Nature
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