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Florencio E. Podestá - One of the best experts on this subject based on the ideXlab platform.

Alberto A. Iglesias - One of the best experts on this subject based on the ideXlab platform.

R. A. H. Vetter - One of the best experts on this subject based on the ideXlab platform.

  • ecophysiological studies on citrate synthase i Enzyme Regulation of selected crustaceans with regard to temperature adaptation
    Journal of Comparative Physiology B-biochemical Systemic and Environmental Physiology, 1995
    Co-Authors: R. A. H. Vetter
    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.

  • Ecophysiological studies on citrate synthase: (II) Enzyme Regulation of selected crustaceans with regard to life-style and the climatic zone
    Journal of Comparative Physiology B, 1995
    Co-Authors: R. A. H. Vetter
    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.

William C. Plaxton - One of the best experts on this subject based on the ideXlab platform.

Karlene A. Cimprich - One of the best experts on this subject based on the ideXlab platform.