Ca-ATPase and Mg-ATPase enzyme activities of the tropical-subtropical starfish Aquilonastra yairi under ocean acidification and warming in the laboratory
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| Natura: | Dataset Open Access |
| Lingua: | en |
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PANGAEA
2024
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| _version_ | 1867168226948939776 |
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| author | Khalil, Munawar Stuhr, Marleen Kunzmann, Andreas Westphal, Hildegard |
| author_facet | Khalil, Munawar Stuhr, Marleen Kunzmann, Andreas Westphal, Hildegard |
| collection | Datos científicos de ciencias marinas y ambientales |
| contents | Enzyme activities involved in biomineralization were determined in the tropical-subtropical starfish Aquilonastra yairi from the culture stock of the ZMT-MAREE laboratory in response to projected near-future global change. To investigate the physicochemical alteration of starfish induced by elevated seawater pCO2 and temperature, starfish of the species A. yairi (342 specimens, size 3-11 mm in diameter, culture stock) were reared in aquaria system under controlled experimental environment conditions at ZMT-MAREE. The starfish were acclimatized to two temperature levels (27 °C, 32 °C) crossed with three pCO2 concentrations (455 µatm, 1052 µatm, 2066 µatm). Protein concentration was determined using the Bradford assay method (Bradford, 1976). Furthermore, Ca-ATPase and Mg-ATPase activities were measured according to protocols initially developed by Chan et al. (1986), Busacker and Chavin (1981) and modified by Prazeres et al. (2015). Positive parabolic responses of Ca-ATPase and Mg-ATPase enzyme activities were detected at 27 °C with elevated pCO2, while stable enzyme activities were observed at 32 °C with elevated pCO2. The calcification-related enzymes Ca-ATPase and Mg-ATPase activity appear to be sensitive to pCO2/pH changes, leading to vulnerability concerning the skeletal structure. |
| format | Dataset Open Access |
| id | pangaea_https___doi_org_10_1594_PANGAEA_965905 |
| institution | PANGAEA |
| language | en |
| publishDate | 2024 |
| publisher | PANGAEA |
| record_format | pangaea |
| spellingShingle | Ca-ATPase and Mg-ATPase enzyme activities of the tropical-subtropical starfish Aquilonastra yairi under ocean acidification and warming in the laboratory Khalil, Munawar Stuhr, Marleen Kunzmann, Andreas Westphal, Hildegard Calcium adenosine triphosphatase activity; Calculated; calculated from carbonate chemistry using the CO2Sys Excel sheet (Pierrot, Lewis & Wallace, 2006); enzyme activity; global change; Laboratory experiment; Magnesium adenosine triphosphatase activity; Multi-parameter portable meter, Xylem Analytics, WTW MultiLine® 3630 IDS; pH; pH, standard deviation; Sample ID; Sampling date/time, experiment; Species, unique identification; Species, unique identification (Semantic URI); Species, unique identification (URI); Spectrophotometer; according to Dickson et al. (2007); Spectrophotometry; starfish; Treatment; Treatment: partial pressure of carbon dioxide; Treatment: temperature; Type of study Enzyme activities involved in biomineralization were determined in the tropical-subtropical starfish Aquilonastra yairi from the culture stock of the ZMT-MAREE laboratory in response to projected near-future global change. To investigate the physicochemical alteration of starfish induced by elevated seawater pCO2 and temperature, starfish of the species A. yairi (342 specimens, size 3-11 mm in diameter, culture stock) were reared in aquaria system under controlled experimental environment conditions at ZMT-MAREE. The starfish were acclimatized to two temperature levels (27 °C, 32 °C) crossed with three pCO2 concentrations (455 µatm, 1052 µatm, 2066 µatm). Protein concentration was determined using the Bradford assay method (Bradford, 1976). Furthermore, Ca-ATPase and Mg-ATPase activities were measured according to protocols initially developed by Chan et al. (1986), Busacker and Chavin (1981) and modified by Prazeres et al. (2015). Positive parabolic responses of Ca-ATPase and Mg-ATPase enzyme activities were detected at 27 °C with elevated pCO2, while stable enzyme activities were observed at 32 °C with elevated pCO2. The calcification-related enzymes Ca-ATPase and Mg-ATPase activity appear to be sensitive to pCO2/pH changes, leading to vulnerability concerning the skeletal structure. |
| title | Ca-ATPase and Mg-ATPase enzyme activities of the tropical-subtropical starfish Aquilonastra yairi under ocean acidification and warming in the laboratory |
| topic | Calcium adenosine triphosphatase activity; Calculated; calculated from carbonate chemistry using the CO2Sys Excel sheet (Pierrot, Lewis & Wallace, 2006); enzyme activity; global change; Laboratory experiment; Magnesium adenosine triphosphatase activity; Multi-parameter portable meter, Xylem Analytics, WTW MultiLine® 3630 IDS; pH; pH, standard deviation; Sample ID; Sampling date/time, experiment; Species, unique identification; Species, unique identification (Semantic URI); Species, unique identification (URI); Spectrophotometer; according to Dickson et al. (2007); Spectrophotometry; starfish; Treatment; Treatment: partial pressure of carbon dioxide; Treatment: temperature; Type of study |
| url | https://doi.org/10.1594/PANGAEA.965905 |