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  • 1
    Digitale Medien
    Digitale Medien
    Charge trapping in the reductive dissolution of colloidal suspensions of iron(III) oxides (1988)
    s.l. : American Chemical Society
    Langmuir 4 (1988), S. 1206-1211 
    Details
    ISSN: 1520-5827
    Quelle: ACS Legacy Archives
    Thema: Chemie und Pharmazie
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1021/la00083a028
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  • 2
    Digitale Medien
    Digitale Medien
    The utilisation of d-galactonate and d-2-oxo-3-deoxygalactonate by Escherichia coli K-12 (1978)
    Springer
    Archives of microbiology 118 (1978), S. 199-206 
    Details
    ISSN: 1432-072X
    Schlagwort(e): E. coli K-12 ; Galactonate ; 2-Oxo-3-deoxygalactonate ; Genetic mapping
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract 1. Escherichia coli K-12 mutants unable to grow on d-galactonate have been isolated and found to be defective in either galactonate dehydratase, 2-oxo-3-deoxygalactonate 6-phosphate aldolase or devoid of both of these enzymes and of 2-oxo-3-deoxygalactonate kinase. 2. 2-Oxo-3-deoxygalactonate kinase and 2-oxo-3-deoxygalactonate 6-phosphate aldolase are still induced by galactonate in mutants lacking galactonate dehydratase, suggesting that galactonate rather than a catabolic product of galactonate is the inducer of the galactonate catabolic enzymes. Synthesis of the enzymes is subject to glucose catabolite repression. 3. Mutants defective in 2-oxo-3-deoxygalactonate 6-phosphate aldolase accumulate 2-oxo-3-deoxygalactonate 6-phosphate when exposed to galactonate and this compound causes general growth inhibition. 4. Secondary mutants that no longer show this inhibition fail to make 2-oxo-3-deoxygalactonate 6-phosphate due to additional defects in galactonate transport, galactonate dehydratase, 2-oxo-3-deoxygalactonate kinase or a putative promoter mutation that prevents formation of these enzymes. 5. A spontaneous mutant capable of growth on 2-oxo-3-deoxygalactonate has been isolated. It has two genetically distinct mutations. One permits constitutive formation of the galactonate catabolic enzymes and the other allows the uptake of 2-oxo-3-deoxygalactonate. Neither mutation on its own permitted growth on 2-oxo-3-deoxygalactonate. 6. Genes specifying the various galactonate catabolic enzymes have been located at min 81.7 on the E. coli K-12 linkage map and probably constitute an operon. The gene sequence in this region was shown to by: pyrE uhp dgo dnaA.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00415730
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  • 3
    Digitale Medien
    Digitale Medien
    Catabolism of 3-hydroxybenzoate by the gentisate pathway in Klebsiella pneumoniae M5a1 (1990)
    Springer
    Archives of microbiology 154 (1990), S. 489-495 
    Details
    ISSN: 1432-072X
    Schlagwort(e): Klebsiella pneumoniae M5a1 ; 3-Hydroxybenzoate degradation ; Gentisate pathway ; 3-Hydroxybenzoate monooxygenase mutants ; Maleylpyruvate isomerase mutants
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract Growth of Klebsiella pneumoniae M5a1 on 3-hydroxybenzoate leads to the induction of 3-hydroxybenzoate monooxygenase, 2,5-dihydroxybenzoate dioxygenase, maleylpyruvate isomerase and fumarylpyruvate hydrolase. Growth in the presence of 2,5-dihydroxybenzoate also induces all of these enzymes including the 3-hydroxybenzoate monooxygenase which is not required for 2,5-dihydroxybenzoate catabolism. Mutants defective in 3-hydroxybenzoate monooxygenase fail to grow on 3-hydroxybenzoate but grow normally on 2,5-dihydroxybenzoate. Mutants lacking maleylpyruvate isomerase fail to grow on 3-hydroxybenzoate and 2,5-dihydroxybenzoate. Both kinds of mutants grow normally on 3,4-dihydroxybenzoate. Mutants defective in maleylpyruvate isomerase accumulate maleylpyruvate when exposed to 3-hydroxybenzoate and growth is inhibited. Secondary mutants that have additionally lost 3-hydroxybenzoate monooxygenase are no longer inhibited by the presence of 3-hydroxybenzoate. The 3-hydroxybenzoate monooxygenase gene (mhbM) and the maleylpyruvate isomerase gene (mhbI) are 100% co-transducible by P1 phage.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00245233
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  • 4
    Digitale Medien
    Digitale Medien
    An Escherichia coli mutant defective in the NAD-dependent succinate semialdehyde dehydrogenase (1982)
    Springer
    Archives of microbiology 132 (1982), S. 270-275 
    Details
    ISSN: 1432-072X
    Schlagwort(e): Escherichia coli ; Succinate semialdehyde dehydrogenase ; Aromatic catabolism ; Hydroxyphenylacetate ; Genetic mapping
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract Escherichia coli mutants, unable to grown on 4-hydroxyphenylacetate, have been isolated and found to be defective in the NAD-dependent succinate semialdehyde dehydrogenase. When the mutants are grown with 4-aminobutyrate as sole nitrogen source an NAD-dependent succinate semialdehyde dehydrogenase seen in the parental strain is absent but, as in the parental strain, an NADP-dependent enzyme is induced. Growth of the mutants is inhibited by 4-hydroxyphenylacetate due to the accumulation of succinate semialdehyde. The mutants are more sensitive to inhibition by exogenous succinate semialdehyde than is the parental strain. Secondary mutants able to grow in the presence of 4-hydroxyphenylacetate but still unable to use it as sole carbon source were defective in early steps of 4-hydroxyphenylacetate catabolism and so did not form succinate semialdehyde from 4-hydroxyphenylacetate. The gene encoding the NAD-dependent succinate semialdehyde dehydrogenase of Escherichia coli K-12 was located at min 34.1 on the genetic map.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00407964
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  • 5
    Digitale Medien
    Digitale Medien
    Time resolved luminescence spectroscopy of alkaline earth oxides after pulsed electron beam irradiation. II. Spectra and thresholds of MgO (1989)
    College Park, Md. : American Institute of Physics (AIP)
    The Journal of Chemical Physics 90 (1989), S. 807-812 
    Details
    ISSN: 1089-7690
    Quelle: AIP Digital Archive
    Thema: Physik , Chemie und Pharmazie
    Notizen: Time-resolved luminescence spectroscopy has been used to study the emissions occurring in MgO in the time range 100 ns to 100 μs after irradiation with nanosecond duration pulses of electrons of energy between 0.2 and 3.0 MeV. An emission at ∼380 nm with a threshold energy of 0.28±0.01 MeV is attributed to processes resulting from the displacement of oxygen anions and the formation of F+ centers. An emission at ∼240 nm is attributed to processes resulting from the displacement of magnesium cations, with a threshold energy of 0.32±0.01 MeV. An emission at ∼470 nm at an electron energy of 3.0 MeV is attributed to processes resulting from the formation of aggregates of F+ centers, such as the F2+2 center. Displacement energies of 49±2 and 38±2 eV were estimated for oxygen anions and magnesium cations, respectively.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1063/1.456105
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  • 6
    Digitale Medien
    Digitale Medien
    A temperature effect in the luminescence emission from electron-irradiated MgO (1990)
    College Park, Md. : American Institute of Physics (AIP)
    The Journal of Chemical Physics 92 (1990), S. 6441-6446 
    Details
    ISSN: 1089-7690
    Quelle: AIP Digital Archive
    Thema: Physik , Chemie und Pharmazie
    Notizen: The temperature dependence of luminescence emissions from electron-irradiated CaO and MgO single crystals has been studied by time resolved luminescence spectroscopy after pulsed nanosecond irradiation with 0.20 to 0.60 MeV electrons. Emissions from CaO at 375 nm at both 293 and 83 K, show similar threshold characteristics for atomic displacement. These have been attributed to the displacement of oxygen ions and subsequent electron trapping, resulting in the formation of F+ centers. The threshold energy of 0.32±0.01 MeV corresponds to an oxygen displacement energy of 58±2 eV. A 380 nm emission from MgO, also attributed to oxygen displacement and F+ center formation, shows no temperature effect, with a displacement threshold virtually identical to that for CaO. A 235 nm emission from MgO shows a significant temperature effect. The threshold energy at 293 K is 0.31±0.01 MeV, whilst at 83 K two thresholds are observed, 0.31±0.01 and 0.41±0.01 MeV.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1063/1.458596
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  • 7
    Digitale Medien
    Digitale Medien
    Time resolved luminescence spectroscopy of alkaline earth oxides after pulsed electron beam irradiation. I. Spectra and thresholds of CaO and CaO:Mg (1988)
    College Park, Md. : American Institute of Physics (AIP)
    The Journal of Chemical Physics 88 (1988), S. 4158-4170 
    Details
    ISSN: 1089-7690
    Quelle: AIP Digital Archive
    Thema: Physik , Chemie und Pharmazie
    Notizen: Time resolved luminescence spectroscopy has been used to study the emissions occurring in CaO and CaO:Mg in the range 20 ns to 100 ms after irradiation with nanosecond duration pulses of electrons of energy between 0.2 and 3.0 MeV. An emission at 375 nm in pure CaO with a threshold energy of 0.29±0.2 MeV is attributed to processes resulting from the displacement of oxygen anions and the formation of F+ centers. A related emission in CaO:Mg is attributed to displacements involving oxygen anions and the formation of F+Mg centers. An emission at 560 nm observed in both CaO and CaO:Mg with a threshold energy ∼0.7 MeV is attributed to processes resulting from cation displacement. A surprising consequence of these observations is that the displacement energies of oxygen ions in the CaO lattice appear to be lower (∼50 eV for CaO and ∼35 eV in CaO:Mg) than that of the calcium cations (∼65 eV).
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1063/1.453823
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  • 8
    Digitale Medien
    Digitale Medien
    5-Carboxymethyl-2-hydroxymuconic semialdehyde dehydrogenases of Escherichia coli C and Klebsiella pneumoniae M5a1 show very high N-terminal sequence homology (1989)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 57 (1989), S. 0 
    Details
    ISSN: 1574-6968
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Biologie
    Notizen: Abstract 5-Carboxymethyl-2-hydroxymuconic semialdehyde (CHMS) dehydrogenase from Escherichia coli C and Klebsiella pneumoniae M5a1 have been purified and some of their properties studied. The apparent Km values for NAD and CHMS were 11.7 ± 1.5 μM and 5.2 ± 1.9 μM. respectively, for the K. pneumoniae enzyme, and 19.5 ± 2.7 μM and 9.2 ± 1.4 μM, respectively, for the E. coli enzyme. Both enzymes were optimally active at pH 7.5 in sodium phosphate buffer. They had subunit molecular weights of 52 000 (± 1000) and the native enzymes appeared to be dimers of identical subunits. The first 20 residues of their N-terminal amino acid sequences were 90% homologous. A degenerate oligonucleotide probe constructed to a six amino acid sequence common to both enzymes gave strong hybridization with DNA from E. coli strains B and W as well as with E. coli C and K. pneumoniae but little or no hybridization to DNA from E. coli K12 or Pseudomonas putida.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1574-6968.1989.tb03354.x
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  • 9
    Digitale Medien
    Digitale Medien
    Biochemical genetics of aerobactin biosynthesis in Escherichia coli (1986)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 36 (1986), S. 0 
    Details
    ISSN: 1574-6968
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Biologie
    Notizen: Abstract Single-gene mutants of Escherichia coli defective in aerobactin biosynthesis were incubated under non-growing conditions for 2 h with radiolabelled lysine. Analysis of the intermediates produced suggested that acetylation of lysine may be the first step in aerobactin production.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1574-6968.1986.tb01710.x
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  • 10
    Digitale Medien
    Digitale Medien
    formation for phenylethylamine oxidase expressed in Escherichia coli K-12 (1995)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 133 (1995), S. 0 
    Details
    ISSN: 1574-6968
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Biologie
    Notizen: Abstract Arthrobacter globiformis amine oxidase produced by Escherichia coli cells grown in copper-depleted media was reported to undergo activation due to formation of its topaquinone cofactor in a copper-dependent autocatalytic reaction. Likewise, a mutated E. coli amine oxidase located in the cytoplasm was reported to form topaquinone autocatalytically in an EDTA-sensitive reaction. Here we show unequivocally that formation of an amine oxidase lacking topaquinone is primarily a consequence of the location of the enzyme in the cytoplasm rather than the level of copper in the growth medium. For E. coli, insertion of copper into apoamine oxidase and subsequent topaquinone formation occur after export of the apoenzyme into the periplasm.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1574-6968.1995.tb07896.x
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