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  • Acetate metabolism  (1)
  • Dimethylsulfoxide  (1)
  • 1
    Electronic Resource
    Electronic Resource
    A thallium-205 NMR study of thallium acetate ion association in 2,2,2-trifluoroethanol and dimethylsulfoxide (1982)
    Springer
    Journal of solution chemistry 11 (1982), S. 379-386 
    Details
    ISSN: 1572-8927
    Keywords: Dimethylsulfoxide ; thallium acetate ; trifluoroethanol ; Tl-205 NMR chemical shifts
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The association of thallium acetate ion in 2,2,2-trifluoroethanol and dimethyl-sulfoxide has been investigated by thallium-205 NMR spectroscopy. Analysis of the association constants as a function of temperature indicates that in trifluoroethanol the association enthalpy and entropy are, respectively, 1.6 kcal-mol−1 and 19.3 cal-mol−1-K−1 and in dimethylsulfoxide they are-0.99 kcal-mol−1 and 18.0 cal-mol−1-K−1. Examination of the temperature dependence of the chemical shift of the ion-pair reveals that in dimethylsulfoxide the ion-pair exists as a contact species, while in trifluoroethanol the solvent-separated ion-pair is more likely.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00649036
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Characterization of the glyoxysomal isocitrate lyase genes of Aspergillus nidulans (acuD) and Neurospora crassa (acu-3) (1992)
    Springer
    Current genetics 21 (1992), S. 43-47 
    Details
    ISSN: 1432-0983
    Keywords: Aspergillus ; Neurospora ; Isocitrate lyase ; Glyoxysome ; Acetate metabolism
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The nucleotide sequences of the genes encoding the acetate-inducible glyoxylate cycle enzyme isocitrate lyase from the ascomycete fungi Aspergillus nidulans (acuD) and Neurospora crassa (acu-3) are presented. The respective A. nidulans and N. crassa genes are interrupted at identical positions by two introns and encode proteins of 538 and 543 amino acids, which have 75% identity. The predicted protein sequences do not demonstrate the C-terminal tripeptide S-K-L that has been implicated in peroxisomal targeting and found in the glyoxysomally located enzyme malate synthase from the same species. However, the protein sequences do exhibit a partial repeat which, in common with malate synthase, is located in regions that are absent from, or non-homologous with, the E. coli enzyme, which is not compartmentalized.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00318653
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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