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  • Thiamine pyrophosphate enzymes  (1)
  • polyampholytes  (1)
  • 1
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 38 (1991), S. 1012-1019 
    ISSN: 0006-3592
    Keywords: invertase ; polyelectrolytes ; polyampholytes ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: In connection with our work on polyelectrolyte complex formation with polyampholytes, the interaction between invertase and several linear polyelectorlytes has been investigated by means of turbidimetry, light scattering measurements, and determination of the enzyme activity. Polyelectrolyte complex formation of invertase was shown to occur with cationic polyelectrolytes only. The light-scattering data yield information on aggregation and desegregation processes in complex formation. As indicated by our results, only a part of the protein molecules is engaged in this Coulombic interaction, and this part shows a rather small enzyme activity only. Thus, a direct interaction between invertase and a cationic polyelectrolyte is no effective approach to enzyme binding, but a complete immobilization of invertase can be achieved via an “inclusion flocculation” with a symplex formed by interaction between an anionic and a cationic linear polyelectrolyte or via immobilization in symplex microcapsules.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Weinheim : Wiley-Blackwell
    Berichte der deutschen chemischen Gesellschaft 123 (1990), S. 1489-1494 
    ISSN: 0009-2940
    Keywords: Thiamine pyrophosphate enzymes ; Thiamine pyrophosphate mechanism ; Substitutions, site-directed ; Chemistry ; Inorganic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The Function of the 4′-Aminopyrimidine Component in the Mechanism of the Catalysis of Thiamine Pyrophosphate Enzymes from Today's ViewBinding mechanism and coenzyme function of thiamine pyrophosphate (TPP) are described with the help of site-directed substitutions at different positions of the coenzyme. In accordance to the earlier suggestions of Langenbeck (see this issue2) it is shown, that besides the thiazolium moiety (C2 atom) also the aminopyrimidine part plays an essential role in the catalytic mechanism of TPP enzymes such as pyruvate decarboxylase, pyruvate dehydrogenase, and transketolase, respectively. A two-center mechanism of TPP is proposed explaining the function of the amino group as an internal proton relay in the catalytic mechanisms of TPP enzymes.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    Location Call Number Limitation Availability
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