Enzyme activities of Calanus finmarchicus from the North Atlantic collected during Maria S. Merian cruise MSM26 in spring 2013

• Main Authors: Schmithüsen, Tosia, Niehoff, Barbara, Auel, Holger
• Format: Dataset
• Language: English
• Published: PANGAEA 2014
• Subjects: Absorbance of control; Absorbance of sample; Basin Scale Analysis; Synthesis and Integration; Citrate synthase activity; dry mass; Citrate synthase activity per individual; Date; Date/Time of event; Depth; bottom/max; top/min; water; D-MOC; Double opening/closing plankton net; EURO-BASIN; Event label; Latitude of event; Life stage; Lipase activity; Lipase activity per individual; Longitude of event; Maria S. Merian; MSM26; MSM26_126-9; MSM26_127-17; MSM26_127-19; MSM26_131-17; MSM26_133-6; MSM26_134-19; MSM26_135-16; MSM26_136-8; North Atlantic Ocean; Number of individuals; Proteinase activity; per dry mass; Delta extinction at 366 nm; Proteinase activity per individual; Sample ID; Spectrophotometer Thermo Scientific UV1; Taxon/taxa; Treatment; Treatment: temperature; Uniform resource locator/link to reference; WP2; WP-2 towed closing plankton net; Calanus finmarchicus; North Atlantic; Copepods
• Online Access: https://doi.pangaea.de/10.1594/PANGAEA.835177; https://doi.org/10.1594/PANGAEA.835177

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.