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  • Enzymes
  • Wiley-Blackwell  (3)
  • 1980-1984  (1)
  • 1965-1969  (2)
  • 1925-1929
  • 1983  (1)
  • 1967  (2)
  • 1
    ISSN: 0570-0833
    Keywords: Acetylcholin esterase ; Enzymes ; Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Acetylcholinesterase plays a vital part in the functioning of nerves, and serious physiological damage arises from its blockage by esters of phosphonic and phosphoric acid used e. g. in pesticides. The properties and the mechanism of action of acetylcholinesterase, which show many similarities to those of other hydrolases, are described. Therapeutic agents (reactivators) for the toxic phosphorus compounds specified are also discussed.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Weinheim : Wiley-Blackwell
    Angewandte Chemie International Edition in English 22 (1983), S. 275-283 
    ISSN: 0570-0833
    Keywords: Cytochrome c oxidase ; Enzymes ; Warburg, Otto ; Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Approximately 50 years ago, Otto Warburg received the Nobel Prize for his fundamental work on the “Atmungsferment”. But not until the end of the fifties was it possible to isolate this complicated membrane enzyme, which is necessary for respiration and energy production in most living organisms on earth. Since then, intensive research has been performed to elucidate the mechanism of reduction of oxygen to water and the coupled translocation of protons across the membrane which is involved in ATP synthesis. Until now the results have been unsatisfactory because the four catalytic heavy-metal redox centers are bound to proteins, the structures of which have begun to be studied only recently. In the course of this research, it was discovered that cytochrome c oxidase from bacteria contains only two or three, whereas the enzyme complex from animals contains thirteen different protein components. The present article analyzes the possible functions of the various protein subunits and, using the example of cytochrome c oxidase, shows that biochemical evolution proceeds in such a way as to increase regulatory capacity.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Weinheim : Wiley-Blackwell
    Angewandte Chemie International Edition in English 6 (1967), S. 1024-1035 
    ISSN: 0570-0833
    Keywords: Active centers ; Pyruvate decarboxylase ; Enzymes ; Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Kinetic studies have shown that the two low molecular-weight components of yeast pyruvate decarboxylase (thiamine pyrophosphate and Mg2⊕ ions) first add rapidly and reversibly to the apoenzyme in binary equilibria. The resulting adduct then “cyclizes” in a rate-determining, practically irreversible reaction to form the thermodynamically stable holoenzyme. These results were supplemented and extended by the testing of numerous analogues of thiamine pyrophosphate in enzyme experiments and then used for the interpretation of the enzyme reaction.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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