3 resultados para enzyme synthesis

em Publishing Network for Geoscientific


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The present study aimed to contribute to the knowledge on the intraspecific variations of enzyme activities in populations of Calanus finmarchicus from different longitudes across the North Atlantic Ocean and their relation to changing environmental conditions. C. finmarchicus was sampled across the North Atlantic in basins with decreasing temperature regimes from east to west (Iceland Basin, Irminger Basin and Labrador Basin) in late March/early April 2013. Potential maximum enzyme activities of digestive (proteinases and lipases/esterases) and metabolic (citrate synthase) enzymes of copepods from all sampling stations were analysed and thermal profiles (5-50°C) of enzyme activities were determined. In order to investigate its acclimation potential, C. finmarchicus were acclimated to 4°C and 15°C for two weeks and thermal profiles of enzyme activities were compared afterwards.

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The activities of proteinases, lipases/esterases and citrate synthase of Calanus finmarchicus copepodites (CV) were analysed. Analysis was performed at 30°C for copepods from seven stations (126-9, 127-17, 131-17, 133-6, 134-19, 135-16, 136-8). In addition, thermal profiles (5-50°C) of these enzymes were analysed for copepods from 3 stations (127-17, 133-6, 135-16). C. finmarchicus of station 127-19 have been acclimated on board to two different temperatures (4 and 15°C) for two weeks. Thermal profiles (5-60°C) of lipases/esterases and proteinases of adult females from each treatment were analysed. Groups of 10 individuals were used to prepare enzyme extracts for analysis. From each station/treatment, three groups were analysed, each of which was measured in triplicates. The activity of proteinases was determined photometrically after Saborowski et al. (2004, hdl:10013/epic.20836), modified after Kreibich et al. (2008, doi:10.1007/s10152-008-0112-0). Azocasein was used as substrate. The lypolytic activity of lipases and esterases in the extract was analysed fluorometrically after Knotz et al. (2006, doi:10.1016/j.cbpa.2006.07.019) using 4-methylumbelliferyl butyrate as substrate. Citrate synthase activity was analysed photometrically after Stitt (1984) modified by Saborowski and Buchholz (2002) with oxaloacetic acid as substrate. For detailed description please contact the author.

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Effects of severe hypercapnia have been extensively studied in marine fishes, while knowledge on the impacts of moderately elevated CO2 levels and their combination with warming is scarce. Here we investigate ion regulation mechanisms and energy budget in gills from Atlantic cod acclimated long-term to elevated PCO2 levels (2500 µatm) and temperature (18 °C). Isolated perfused gill preparations established to determine gill thermal plasticity during acute exposures (10-22 °C) and in vivo costs of Na+/K+-ATPase activity, protein and RNA synthesis. Maximum enzyme capacities of F1Fo-ATPase, H+-ATPase and Na+/K+-ATPase were measured in vitro in crude gill homogenates. After whole animal acclimation to elevated PCO2 and/or warming, branchial oxygen consumption responded more strongly to acute temperature change. The fractions of gill respiration allocated to protein and RNA synthesis remained unchanged. In gills of fish CO2-exposed at both temperatures, energy turnover associated with Na+/K+-ATPase activity was reduced by 30% below rates of control fish. This contrasted in vitro capacities of Na+/K+-ATPase, which remained unchanged under elevated CO2 at 10 °C, and earlier studies which had found a strong upregulation under severe hypercapnia. F1Fo-ATPase capacities increased in hypercapnic gills at both temperatures, whereas Na+/K+ATPase and H+-ATPase capacities only increased in response to elevated CO2 and warming indicating the absence of thermal compensation under CO2. We conclude that in vivo ion regulatory energy demand is lowered under moderately elevated CO2 levels despite the stronger thermal response of total gill respiration and the upregulation of F1Fo-ATPase. This effect is maintained at elevated temperature.