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  • 1955-1959  (4)
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Naunyn-Schmiedeberg's archives of pharmacology 229 (1956), S. 568-579 
    ISSN: 1432-1912
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Butazolidin (Phenylbutazone) inhibits the oxidative decarboxylation of pyruvate and α-ketoglutarate in a final concentration of 10 mg-% (3,24 · 10−4 m). Data are presented suggesting that the β-ketothiolase is inhibited. The following enzymes or enzyme systems are not inhibited: The enzymes of the respiratory chain, the enzymes of the citric acid cycle with exception of α-ketoglutaric oxidase, the glycolysis of hexosediphosphate (slight inhibition), acetate thiokinase, sulfanilamid transacetylase, pyruvic decarboxylase from yeast, arginase, xanthine oxidase, and D-amino acid oxidase.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Naturwissenschaften 43 (1956), S. 402-403 
    ISSN: 1432-1904
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Natural Sciences in General
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Naunyn-Schmiedeberg's archives of pharmacology 231 (1957), S. 254-261 
    ISSN: 1432-1912
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Glutamic dehydrogenase of rat liver mitochondria is inhibited by phenylbutazone at a final concentration of 2,5 mg-% (0,81 · 10−4 M). However, glutamic dehydrogenase in heart muscle homogenate and the cristalline enzyme from liver are not inhibited by phenylbutazone up to 10 mg-% (3,24 · 10−4 M), but they are inhibited by a metabolite arising during incubation of liver mitochondria with phenylbutazone. A p-hydroxyphenil derivative of phenylbutazone also inhibits glutamie dehydrogenase from heart muscle homogenate and the cristalline enzyme. Phenylbutazone does not act on the purified α-ketoglutaric oxydase system although α-ketoglutaric oxydation by intact rat liver mitochondria is inhibited. The reason for this discrepancy remains open.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Naunyn-Schmiedeberg's archives of pharmacology 229 (1956), S. 495-504 
    ISSN: 1432-1912
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The effect of lead on the reactions of the citric acid cycle, the fatty acid cycle and on anaerobic glycolysis has been studied. The oxidative decarboxylation of pyruvate and α-ketoglutarate is shown to be inhibited. The other reactions of the citric acid cycle are not inhibited. The fatty acid oxidation is inhibited between the activation step and the β-ketothiolase reaction. The anaerobic glycolysis of hexosediphosphate is not inhibited. The results indicate that the respiratory chain is unaffected by lead.
    Type of Medium: Electronic Resource
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