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Mesopelagic fish were collected using a 1 m**2 Double-MOCNESS (Multiple Opening and Closing Net and Environmental Sensing System) and 4.5 m**2 IKMT (Isaacs-Kidd midwater trawl). The main portion of the IKMT was 20 mm knotted nylon, and the tail bag was 3 mm knotless nylon. Oblique IKMT tows were made to a maximum depth of 500 m at a tow speed of 3.5 knots. The original cruise plan intended for nighttime IKMT tows, but tow times varied due to operational constraints. The MOCNESS was equipped with 20 nets of 333 µm mesh size; 10 nets per side. The towing speed was 2 knots. Samples were collected to a maximum depth of 1250 m. The first oblique nets sampled from the surface to the max depth, and the other nets sampled depth stratified bins of the water column. MOCNESS hauls were performed during day and night to investigate diel vertical migrations. Mesoplelagic fish were processed on board. All fish were picked from all IKMT nets, most oblique MOCNESS nets, and the left side nets of the depth stratified MOCNESS samples. The Depth stratified nets from the right side of the MOCNESS frame were preserved in 5 % formalin for future quantitative analyses of the nekton. Fish were identified to the lowest possible taxa using Whitehead et al. (1984) and Fahay (2007). Standard length of each fish was measured to the nearest 0.1 mm using a digital caliper. Measured and identified fish were frozen in an -80 °C freezer, and shipped to the University of Hamburg at the end of the cruise.

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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.