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  • Electronic Resource  (3)
  • General Chemistry  (2)
  • Adverse Effects  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Adverse drug reactions and debrisoquine/sparteine (P450IID6) polymorphism in patients with fibromyalgia (1997)
    Springer
    Clinical rheumatology 16 (1997), S. 291-295 
    Details
    ISSN: 1434-9949
    Keywords: Fibromyalgia ; Adverse Effects ; P450IID6 Polymorphism
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Objective: To assess the frequency of adverse drug reaction in patients with fibromyalgia in relation to medications prescribed for this condition. To evaluate the potential role of the P450IID6 phenotype in the pathogenesis of these adverse drug reactions. Methods: Thirty-five patients with fibromyalgia were assessed using a structured questionnaire with demographic and clinical data and perceived adverse drug reactions. A sample of 60 patients with rheumatoid arthritis and 62 patients with localized back pain served as controls. The P450IID6 phenotype was determined for each of the fibromyalgia patients. Results: Overall, 141 patients had used NSAID and 79 (56%) of them reported adverse effects. Antidepressant drugs were used by 68 patients and 35 (51%) patients had adverse effects. Muscle relaxant drugs were used by 48 patients and 15 (31%) of them reported side effects. Analgesics were used by 122 patients and 22 (18%) had experienced adverse effects. Statistical differences in the frequency of adverse effects were found with antidepressant drugs in the fibromyalgia group, compared with rheumatoid arthritis (p=0.01) and back pain (p=0.02). Four of the 35 patients (11.4%) had a metabolic ratio (M.R.) greater than 0.30 (log M.R.=−0.52) indicative of the poor metabolizers (PM) phenotype. M.R. varied from 0.005 (log M.R.=−2.30) to 4.99 (log M.R.=0.70). Conclusions: The problem of adverse drug reactions in fibromyalgia patients does not appear to correlate with the PM phenotype of the P450IID6 oxidative enzyme. It also is unlikely that altered xenobiotic detoxification attributable to this PM phenotype would have a significant role in the development of fibromyalgia.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02238966
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  • 2
    Electronic Resource
    Electronic Resource
    Eisen-Schwefel-Proteine: Strukturchemie ihrer Chromophore und verwandter Systeme (1973)
    Weinheim : Wiley-Blackwell
    Zeitschrift für die chemische Industrie 85 (1973), S. 390-400 
    Details
    ISSN: 0044-8249
    Keywords: Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Intensive Untersuchungen an Eisen-Schwefel-Proteinen wurden erst vor etwa einem Jahrzehnt begonnen, doch haben sich seither auf diesem Gebiet viele biologische und physikalisch-chemische Einzelerkenntnisse angesammelt, die auch in Übersichtsarbeiten zusammengestellt worden sind[1-5]. Als Ergebnis der Röntgen-Strukturanalysen von Rubredoxin[6], Ferredoxin (Peptococcus aerogenes)[7] und des Eisen-Proteins aus Chromatium vinosum mit hohem Normalpotential (high potential iron protein, HIPIP)[8] kann man jetzt eine Übersicht über Natur und Funktion der anorganischen Chromophore in diesen Proteinen geben, diese Befunde mit „Modell“-Systemen von wechselnder Relevanz in Beziehung setzen sowie Redox-prozesse in biologischen Systemen besonders im Hinblick darauf erläutern, was man allosterische Effekte auf die Elektronenübertragung in Metallenzymen nennen könnte.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/ange.19730850904
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  • 3
    Electronic Resource
    Electronic Resource
    Iron-Sulfur Proteins: Structural Chemistry of Their Chromophores and Related Systems (1973)
    Weinheim : Wiley-Blackwell
    Angewandte Chemie International Edition in English 12 (1973), S. 390-399 
    Details
    ISSN: 0570-0833
    Keywords: Iron-sulfur proteins ; Proteins ; Chromophores ; Bioinorganic chemistry ; Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Intensive studies of iron-sulfur proteins were begun only a decade or so ago but many biological and physicochemical data have since been accumulated and summarized[1-5]. As a result of the very recent X-ray analyses of the structures of rubredoxin[6], ferredoxin (Peptococcus aerogenes)[7] and the Chromatium vinosum high potential iron protein (Hipip)[8], it has become possible to review our understanding of the nature and function of the inorganic chromophores in these proteins; to relate these findings to ‘model’ systems of varying relevance; but of more general interest, to comment on redox processes in biological systems particularly with respect to what might be termed electron transfer - allosteric effects in metalloenzymes.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/anie.197303901
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    Paper (German National Licenses)
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