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  • 1985-1989  (2)
  • 1980-1984  (1)
  • 1965-1969
  • 1960-1964
  • 1986  (2)
  • 1984  (1)
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  • 1985-1989  (2)
  • 1980-1984  (1)
  • 1965-1969
  • 1960-1964
Year
Keywords
  • 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
  • 3
    Electronic Resource
    Electronic Resource
    Immobilization of enzymes in porous supports: Effects of support-enzyme solution contacting (1984)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 26 (1984), S. 892-900 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Proteins have been immobilized in porous support particles held in a fixed-bed reactor through which protein solution is continuously circulated. Changing the recirculation flow rate alters the observed immobilization kinetics and the maximum enzyme loading which can be achieved for glucose oxidase and glucoamylase on carbodiimide-treated activated carbon and for glucoamylase immobilized on CNBr-Sepharose 4B. Direct microscopic examination of FITC-labelled protein in sectioned Sepharose particles and indirect activity-loading studies with activated carbon-enzyme conjugates all indicate that immobilized enzyme is increasingly localized near the outer surface of the support particles at larger recirculation flow rates. Restricted diffusion of enzymes may be implicated in this phenomenon. These contacting effects may be significant considerations in the scaleup of processes for protein impregnation in porous supports, since apparent activity and stability of the final preparation depend on internal protein distribution.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260260812
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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