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  • ATP inhibition  (1)
  • As, Se, Hg  (1)
  • Springer  (2)
  • American Chemical Society
  • American Heart Association (AHA)
  • Blackwell Publishing Ltd
  • National Academy of Sciences
  • Nature Publishing Group (NPG)
  • Oxford University Press
  • 2010-2014
  • 1995-1999  (2)
  • 1970-1974
  • 1925-1929
  • 1915-1919
  • 1995  (2)
  • 1971
Document type
Keywords
Publisher
  • Springer  (2)
  • American Chemical Society
  • American Heart Association (AHA)
  • Blackwell Publishing Ltd
  • National Academy of Sciences
    • +
Years
  • 2010-2014
  • 1995-1999  (2)
  • 1970-1974
  • 1925-1929
  • 1915-1919
Year
  • 1995  (2)
  • 1971
  • 1
    Electronic Resource
    Electronic Resource
    Determination of arsenic, selenium and mercury in an estuarine sediment standard reference material using flow injection and atomic absorption spectrometry (1995)
    Springer
    Microchimica acta 118 (1995), S. 163-175 
    Details
    ISSN: 1436-5073
    Keywords: flow injection ; As, Se, Hg ; estuarine sediment ; standard reference material ; microwave-oven digestion ; CVAAS ; FIA-AAS
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract A flow-injection analysis atomic absorption spectrometric (FIA-AAS) method was developed for the determination of trace amounts of arsenic, selenium and mercury in a proposed estuarine sediment standard reference material (SRM 1646a). The samples were prepared in two manners: a) A wet digestion procedure with HNO3, H2SO4, and HClO4 using a reflux column and b) A microwave-oven digestion procedure utilizing HNO3, H2SO4, and HCl for As and Se, and HNO3 for Hg. Microwave-oven digestion provides results comparable to those found by reflux column digestion and reduces the sample preparation time by a factor of 10. The proposed method employing the microwave-oven digestion procedure coupled with FIA-AAS for As and Se, and FIA-CVAAS for Hg, has detection limits of 0.15 ng As/ml, O.17 ng Se/ml and 0.15 ng Hg/ml.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01244356
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Ecophysiological studies on citrate synthase: (II) enzyme regulation of selected crustaceans with regard to life-style and the climatic zone (1995)
    Springer
    Journal of comparative physiology 165 (1995), S. 56-61 
    Details
    ISSN: 1432-136X
    Keywords: Citrate synthase ; Enzyme regulation ; Temperature adaptation ; ATP inhibition ; Crustacea
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Citrate synthase is a regulatory enzyme of the energy metabolism pathway controlling the citric acid cycle. It was studied in order to determine modes of enzyme regulation with regard to the life-style of the investigated species. Citrate synthase from crustaceans with different life-styles were compared: the pelagic euphausiids Euphausia superba from the Antarctic and Meganyctiphanes norvegica from the Scandinavian Kattegat and the Mediterranean were compared to the benthic isopods Serolis polita from the Antarctic and Idotea baltica from the Baltic. Citrate synthase was partly purified chromatographically and the influence of adenosine 5′-triphosphate on enzyme activity was examined. Mechanisms of inhibition and inhibitor constants were determined. Two different mechanisms of enzyme regulation by ATP were found. Citrate synthase from isopods was only competitively inhibited, while citrate synthase from euphausiids showed not only competitive inhibition but also activation by low concentrations of ATP. This activation is equivalent to the reversed methanism of uncompetitive inhibition. The ecophysiological relevances of the coupling of these mechanisms are discussed. The degree of competitive inhibition was different in the two groups of investigated crustaceans. Inhibitor constants were similar within the euphausiids but not in isopods, which showed higher or lower inhibition depending on the climatic zone: the colder the ambient temperature the lower the ATP inhibition. A possible mechanism of temperature adaptation through effects of varying inhibition constants is concluded.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00264686
    Location Call Number Limitation Availability
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    Paper (German National Licenses)
    Fulltext
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