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  • 1
    Electronic Resource
    Electronic Resource
    Skeletal isomerization of 1-butene over mesoporous materials (1999)
    Springer
    Catalysis letters 57 (1999), S. 209-215 
    Details
    ISSN: 1572-879X
    Keywords: 1-butene ; skeletal isomerization ; mesoporous material ; acid site concentration ; monomolecular reaction
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract On the skeletal isomerization of 1-butene, mesoporous materials with mesopores too large to expect any shape selectivity have been used in order to investigate the effects of the concentration of acid sites on the conversion of 1-butene and the selectivity for isobutene. The concentrations of acid sites can be varied through the control of the Si/Al ratio. The conversion of 1-butene increases with increasing the aluminium content of mesoporous materials, while the selectivity for isobutene decreases. The results of ammonia TPD, IR measurement of 1-butene adsorption, and TG analysis of used catalysts indicate that distant location of activated 1-butene molecules induces the monomolecular reaction over the mesoporous materials with low aluminium content, resulting in high selectivity for skeletal isomerization. On the mesoporous material with high aluminium content, however, the high concentration of activated 1-butene molecules accelerates the multimolecular oligomerization and, thus, reduces the selectivity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1019028522765
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Influence of the fluorine loading level on the skeletal isomerization of 1-butene over fluorine-modified alumina (1998)
    Springer
    Catalysis letters 51 (1998), S. 101-107 
    Details
    ISSN: 1572-879X
    Keywords: 1-butene ; skeletal isomerization ; fluorine-modified alumina ; acid site concentration ; monomolecular reaction
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract γ-alumina catalysts modified with different weight loadings of fluorine have been used for skeletal isomerization of 1-butene in order to investigate the effects of the fluorine loading level on the conversion of 1-butene and the selectivity to isobutene formation. Increasing the actual loading of fluorine up to 0.012 wt% led to an increase in conversion of 1-butene over fluorine-modified γ-alumina catalysts, while the high selectivity to isobutene remains almost unchanged. On the other hand, a clear trend of increasing 1-butene conversion with a decreasing selectivity to isobutene is observed for the γ-alumina catalysts with higher loadings of fluorine. An analysis of the results from the thermal analysis, NH3 temperature-programmed desorption, infrared and the 1-butene sorption measurments clearly indicates that the number of strong acid sites in the modified γ-alumina catalysts is greatly enhanced at fluorine loadings higher than 0.012 wt%, leading to the acceleration of 1-butene oligomerization followed by cracking to light hydrocarbons. Therefore, the 1-butene isomerization selectivity from fluorine-modified γ-alumina catalysts can be understood in terms of a competition between the monomolecular and bimolecular reaction pathways, which highly depend on the concentration of strong acid sites.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1019037017971
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Molecular cloning, expression, and functional characterization of a 2Cys-peroxiredoxin in Chinese cabbage (1999)
    Springer
    Plant molecular biology 40 (1999), S. 825-834 
    Details
    ISSN: 1573-5028
    Keywords: 2Cys-peroxiredoxin ; Chinese cabbage ; expression ; functional characterization ; gene cloning
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A cDNA (C2C-Prx) corresponding to a 2Cys-peroxiredoxin (2Cys-Prx) was isolated from a leaf cDNA library of Chinese cabbage. The predicted amino acid sequence of C2C-Prx has 2 conserved cysteines and several peptide domains present in most of the 2Cys-Prx subfamily members. It shows the highest sequence homology to the 2Cys-Prx enzymes of spinach (88%) and Arabidopsis (86%). Southern analysis using the cDNA insert of C2C-Prx revealed that it consists of a small multigene family in Chinese cabbage genome. RNA blot analysis showed that the gene was predominantly expressed in the leaf tissue of Chinese cabbage seedlings, but the mRNA was generally expressed in most tissues of mature plant, except roots. The expression of C2C-Prx was slightly induced by treatment with H2O2 (100μM) or Fe3+/O2/DTT oxidation system, but not by ABA (50 μM) or GA3 (10 μM). The C2C-Prx is encoded as a preprotein of 273 amino acids containing a putative chloroplast-targeting signal of 65 amino acids at its N-terminus. The N-terminally truncated recombinant protein (ΔC2C-Prx) migrates as a dimer in a non-reducing SDS-polyacrylamide gel and as a monomer in a reducing condition. The ΔC2C-Prx shows no immuno cross-reactivity to antiserum of the yeast thiol-specific antioxidant protein, and vice versa. The ΔC2C-Prx prevents the inactivation of glutamine synthetase and the DNA cleavage in the metal-catalyzed oxidation system. In the yeast thioredoxin system containing thioredoxin reductase, thioredoxin, and NADPH, the ΔC2C-Prx exhibits peroxidase activity on H2O2.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006271823973
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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