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  • 1985-1989  (2)
  • 1980-1984
  • 1965-1969
  • 1960-1964
  • 1986  (2)
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  • 1985-1989  (2)
  • 1980-1984
  • 1965-1969
  • 1960-1964
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  • 1
    Electronic Resource
    Electronic Resource
    EPR and EXAFS studies of glucose isomerase activation by divalent metals (1986)
    Springer
    Bioprocess and biosystems engineering 1 (1986), S. 71-77 
    Details
    ISSN: 1432-0797
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract The interactions of Mn2+ and Co2+ with glucose isomerases from three microbial sources have been studied using various direct physical methods. Co2+ was found to activate each enzyme, although the degree of activation varied significantly for enzymes from different organisms. EPR spectroscopy measurements revealed that dissimilarities in the coordination sphere of enzyme-bound Mn2+ accompanied the differences in enzyme activity. Variations in the EPR spectra of a nitroxide spin label coupled to two of the three isomerases, possibly near their active sites, were also observed. In no case was the EPR spectrum influenced by Co2+ addition, a result discordant with the hypothesis that Co2+ activates the enzyme by inducing a conformational change. The proximal biochemical environment of enzymebound Co2+ was also examined using EXAFS spectroscopy. This method showed that glucose causes notable changes in the ligand environment of the enzyme-bound metal, suggesting the formation of an enzyme-metal-substrate bridge complex. The significance of these results relative to possible reaction mechanisms is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00387498
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Helix formation by poly{bis(hydroxyethyl)-L-glutamine} (1986)
    Springer
    Colloid & polymer science 264 (1986), S. 469-472 
    Details
    ISSN: 1435-1536
    Keywords: Helix-coil transition ; poly(hydroxyalkyl-L-glutamine) ; poly{bis(hydroxyethyl)-L-glutamine}
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
    Notes: Abstract Circular dichroism spectra are reported for poly {bis(hydroxyethyl)-L-glutamine}. Its conformation is predominantly that of a statistical coil at or above ambient temperature in water. It becomes partially helical upon cooling. The helix-forming potential of this polypeptide in water is between that of poly(hydroxyethyl-L-glutamine) and poly(hydroxypropyl-L-glutamine). The polypeptide has a large helix content when the solvent is rich in trifluoroethanol.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01421998
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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