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: Event label; Latitude of event; Longitude of event; Date/Time of event; DEPTH, water; Depth, top/min; Depth, bottom/max; Sample ID; Treatment; Taxon/taxa; Uniform resource locator/link to reference; Life stage; Treatment temperature; Date; Number of individuals; Absorbance of sample; Absorbance of control; Proteinase activity per individual, Delta extinction at 366 nm; Proteinase activity per dry mass, Delta extinction at 366 nm; Lipase activity per individual; Lipase activity, dry mass; Citrate synthase activity per individual; Citrate synthase activity, dry mass; Double opening/closing plankton net; WP-2 towed closing plankton net; Spectrophotometer Thermo Scientific UV1; MSM26; Maria S. Merian; Basin Scale Analysis, Synthesis and Integration EURO-BASIN; Calanus finmarchicus; North Atlantic; Copepods
• Online Access: https://dx.doi.org/10.1594/pangaea.835177; https://doi.pangaea.de/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 ...