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OAS accession Detail for 0291321
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| accessions_id: | 0291321 | archive |
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| Title: | Microbial enzyme activities: peptidase activities in bulk seawater samples from the RV\Polarstern cruise ARKXXVII/3 in the Central Arctic Ocean and Laptev Sea, Aug-Sept. 2012 (NCEI Accession 0291321) |
| Abstract: | This dataset contains data collected on R/V Polarstern during cruise ARK-XXVII-3 from 2012-08-09 to 2012-09-22. These data include depth. The instruments used to collect these data include CTD profiler, Fluorometer, and Niskin bottle. These data were collected by Carol Arnosti of University of North Carolina at Chapel Hill as part of the "Latitudinal and depth-related contrasts in enzymatic capabilities of pelagic microbial communities: Predictable patterns in the ocean? (Patterns of activities)" project. The Biological and Chemical Oceanography Data Management Office (BCO-DMO) submitted these data to NCEI on 2020-04-27. The following is the text of the dataset description provided by BCO-DMO: ARK27-3: Bulk MCA Dataset Description: This dataset includes peptidase activities measured in bulk (not filter-fractionated) seawater. Links to archived CTD data are also provided. Five substrates linked to a 7-amido-4-methyl coumarin (MCA) fluorophore, one amino acid – leucine – and four oligopeptides – the chymotrypsin substrates alanine-alanine-phenylalanine (AAF) and alanine-alanine-proline-phenylalanine (AAPF), and the trypsin substrates glutamine-alanine-arginine (QAR) and glutamic acid-gylcine-arginine (EGR) – were used to measure exo- and endo-acting peptidase activities, respectively. |
| Date received: | 20200427 |
| Start date: | 20120809 |
| End date: | 20120922 |
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| West boundary: | 31.21 |
| East boundary: | 130.5795 |
| North boundary: | 88.809 |
| South boundary: | 79.6502 |
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| Submitting institution: | Biological and Chemical Oceanography Data Management Office |
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| Supplementary information: | Acquisition Description: Water was collected via Niskin bottles mounted on a rosette, equipped with a CTD. Five substrates linked to a 7-amido-4-methyl coumarin (MCA) fluorophore, one amino acid – leucine – and four oligopeptides – the chymotrypsin substrates alanine-alanine-phenylalanine (AAF) and alanine-alanine-proline-phenylalanine (AAPF), and the trypsin substrates glutamine-alanine-arginine (QAR) and glutamic acid-gylcine-arginine (EGR) – were used to measure exo- and endo-acting peptidase activities, respectively. Hydrolysis rates of the substrates were measured as an increase in fluorescence as the fluorophore was hydrolyzed from the substrate over time [as in Hoppe, 1993; Obayashi and Suzuki, 2005]. Incubations with the seven low molecular weight substrates were set up in 4 ml cuvettes. For each substrate, triplicate cuvettes were filled with a total volume of 4 ml seawater for experimental incubations; single cuvettes were filled with 4 ml autoclaved seawater for killed control incubations. Substrate was added 100 micromolar concentrations. Fluorescence was measured over at 0 hrs, 24 h, 48h, and 72 h, using a mini fluorimeter. Hydrolysis rates were calculated from the rate of increase of fluorescence in the incubation over time relative to a set of standards of known concentration of fluorophore. All incubations were conducted at 0 C in the dark. |
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| Metadata version: | 1 |
| Keydate: | 2024-04-19 17:28:37+00 |
| Editdate: | 2024-04-19 17:28:54+00 |