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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Helgoland marine research 50 (1996), S. 539-549 
    ISSN: 1438-3888
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-136X
    Keywords: Cold adaptation ; Enzyme kinetics ; Substrate affinity ; Chitinase ; Antarctic krill, Euphausia superba
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract N-acetyl-β-d-glucosaminidase, a chitin-degrading enzyme, is highly active in the integument and digestive tract of euphausiids. The enzyme was used as a model to compare temperature-dependent enzymatic parameters of Antarctic krill, Euphausia superba, with those of a euphausiid species (Meganyctiphanes norvegica) found in both the Scandinavian Kattegat and the Mediterranean. Other species examined were an Antarctic isopod, Serolis polita, and a tropical crab, Ocypode ryderi. Enzyme isoforms of NAGase were isolated chromatographically. Temperature optimum (between 30 and 53 °C) and activation-energy (47–59 kJ·mol-1) of isoenzymes were generally unrelated to genotypic cold adaptation. Although pH profiles were temperature-dependent, there was no apparent temperature-related control of activities by pH in the experienced physiological range. In contrast, apparent Michaelis constants showed minima at ambient water temperatures (total range: 0.1–0.6 mol·l-1). Potentially, enzyme variants play a role in acclimatisation regulated by Michaelis constants. Apparently, the rate-limiting effects of polar temperatures are partly compensated in the Antarctic crustaceans by construction of enzymes with substrate affinities similar to those of species from warmer climates. The significance of apparent Michaelis constants in evaluating mechanisms of metabolic cold compensation is discussed. Necessary additional experimental approaches are highlighted.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Journal of comparative physiology 165 (1995), S. 46-55 
    ISSN: 1432-136X
    Keywords: Citrate synthase ; Enzyme characteristics ; Temperature adaptation ; Isopod crustacea ; Euphausiid crustacea
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract The characteristics and properties chromatographically purified citrate synthase from the euphausiids Euphausia superba (Antarctica) and Meganyctiphanes norvegica (Scandinavian Kattegat and Mediterranean Sea) and from the isopods Serolis polita (Antarctica) and Idotea baltica (Baltic Sea) were used to elucidate biochemical mechanisms of temperature adaptation. Additionally, maintenance experiments were carried out on the euphausiids to determine mechanisms of short term acclimation. Temperature optima (between 37 and 45°C) were unrelated to genotypic cold adaptation, but the activation energy of the Antarctic krill E. superba (10.9 kJ · mol-1) was only a quarter of that in other species (41.8–45.1 kJ · mol-1). The minima of apparent Michaelis constants (total range: 4–20 μmol · 1-1 oxaloacetate; 7–45 μmol · 1-1 acetyl-coenzyme A) showed no relation to natural conditions, and no distinct pH optimum occurred at ambient temperatures. In contrast, apparent Michaelis constants and specific enzyme activities were related to maintenance temperatures in M. norvegica, but not in E. superba. The differences between M. norvegica and E. superba can be interpreted as adaptations to the changes in ambient temperature with regard to the respective steno- and eurythermic tolerances of these crustaceans.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Journal of comparative physiology 165 (1995), S. 56-61 
    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
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