Temperature Effects on Hemocyanin Oxygen Binding in an Antarctic Cephalopod
The functional relevance of oxygen transport by hemocyanin of the Antarctic octopod Megaleledone senoi and of the eurythermal cuttlefish Sepia officinalis was analyzed by continuous and simultaneous recordings of changes in pH and hemocyanin oxygen saturation in whole blood at various temperatures....
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University of Chicago Pr.
2001
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Online Access: | https://oceanrep.geomar.de/id/eprint/53044/ https://oceanrep.geomar.de/id/eprint/53044/1/3744.pdf https://www.journals.uchicago.edu/doi/abs/10.2307/1543086 https://doi.org/10.2307/1543086 |
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ftoceanrep:oai:oceanrep.geomar.de:53044 2023-05-15T13:40:53+02:00 Temperature Effects on Hemocyanin Oxygen Binding in an Antarctic Cephalopod Zielinski, S. Sartoris, F. J. Pörtner, H. O. 2001 text https://oceanrep.geomar.de/id/eprint/53044/ https://oceanrep.geomar.de/id/eprint/53044/1/3744.pdf https://www.journals.uchicago.edu/doi/abs/10.2307/1543086 https://doi.org/10.2307/1543086 en eng University of Chicago Pr. https://oceanrep.geomar.de/id/eprint/53044/1/3744.pdf Zielinski, S., Sartoris, F. J. and Pörtner, H. O. (2001) Temperature Effects on Hemocyanin Oxygen Binding in an Antarctic Cephalopod. Open Access The Biological Bulletin, 200 (1). pp. 67-76. DOI 10.2307/1543086 <https://doi.org/10.2307/1543086>. doi:10.2307/1543086 info:eu-repo/semantics/openAccess Article PeerReviewed 2001 ftoceanrep https://doi.org/10.2307/1543086 2023-04-07T15:56:55Z The functional relevance of oxygen transport by hemocyanin of the Antarctic octopod Megaleledone senoi and of the eurythermal cuttlefish Sepia officinalis was analyzed by continuous and simultaneous recordings of changes in pH and hemocyanin oxygen saturation in whole blood at various temperatures. These data were compared to literature data on other temperate and cold-water cephalopods (octopods and giant squid). In S. officinalis, the oxygen affinity of hemocyanin changed at ΔP50/°C = 0.12 kPa (pH 7.4) with increasing temperatures; this is similar to observations in temperate octopods. In M. senoi, thermal sensitivity was much smaller (<0.01 kPa, pH 7.2). Furthermore, M. senoi hemocyanin displayed one of the highest levels of oxygen affinity (P50 < 1 kPa, pH 7.6, 0 °C) found so far in cephalopods and a rather low cooperativity (n50 = 1.4 at 0 °C). The pH sensitivity of oxygen binding (Δ log P50/Δ pH) increased with increasing temperature in both the cuttlefish and the Antarctic octopod. At low Po2 (1.0 kPa) and pH (7.2), the presence of a large venous oxygen reserve (43% saturation) insensitive to pH reflects reduced pH sensitivity and high oxygen affinity in M. senoi hemocyanin at 0 °C. In S. officinalis, this reserve was 19% at pH 7.4, 20 °C, and 1.7 kPa O2, a level still higher than in squid. These findings suggest that the lower metabolic rate of octopods and cuttlefish compared to squid is reflected in less pH-dependent oxygen transport. Results of the hemocyanin analysis for the Antarctic octopod were similar to those reported for Vampyroteuthis—an extremely high oxygen affinity supporting a very low metabolic rate. In contrast to findings in cold-adapted giant squid, the minimized thermal sensitivity of oxygen transport in Antarctic octopods will reduce metabolic scope and thereby contribute to their stenothermality. Article in Journal/Newspaper Antarc* Antarctic OceanRep (GEOMAR Helmholtz Centre für Ocean Research Kiel) Antarctic The Antarctic The Biological Bulletin 200 1 67 76 |
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Open Polar |
collection |
OceanRep (GEOMAR Helmholtz Centre für Ocean Research Kiel) |
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ftoceanrep |
language |
English |
description |
The functional relevance of oxygen transport by hemocyanin of the Antarctic octopod Megaleledone senoi and of the eurythermal cuttlefish Sepia officinalis was analyzed by continuous and simultaneous recordings of changes in pH and hemocyanin oxygen saturation in whole blood at various temperatures. These data were compared to literature data on other temperate and cold-water cephalopods (octopods and giant squid). In S. officinalis, the oxygen affinity of hemocyanin changed at ΔP50/°C = 0.12 kPa (pH 7.4) with increasing temperatures; this is similar to observations in temperate octopods. In M. senoi, thermal sensitivity was much smaller (<0.01 kPa, pH 7.2). Furthermore, M. senoi hemocyanin displayed one of the highest levels of oxygen affinity (P50 < 1 kPa, pH 7.6, 0 °C) found so far in cephalopods and a rather low cooperativity (n50 = 1.4 at 0 °C). The pH sensitivity of oxygen binding (Δ log P50/Δ pH) increased with increasing temperature in both the cuttlefish and the Antarctic octopod. At low Po2 (1.0 kPa) and pH (7.2), the presence of a large venous oxygen reserve (43% saturation) insensitive to pH reflects reduced pH sensitivity and high oxygen affinity in M. senoi hemocyanin at 0 °C. In S. officinalis, this reserve was 19% at pH 7.4, 20 °C, and 1.7 kPa O2, a level still higher than in squid. These findings suggest that the lower metabolic rate of octopods and cuttlefish compared to squid is reflected in less pH-dependent oxygen transport. Results of the hemocyanin analysis for the Antarctic octopod were similar to those reported for Vampyroteuthis—an extremely high oxygen affinity supporting a very low metabolic rate. In contrast to findings in cold-adapted giant squid, the minimized thermal sensitivity of oxygen transport in Antarctic octopods will reduce metabolic scope and thereby contribute to their stenothermality. |
format |
Article in Journal/Newspaper |
author |
Zielinski, S. Sartoris, F. J. Pörtner, H. O. |
spellingShingle |
Zielinski, S. Sartoris, F. J. Pörtner, H. O. Temperature Effects on Hemocyanin Oxygen Binding in an Antarctic Cephalopod |
author_facet |
Zielinski, S. Sartoris, F. J. Pörtner, H. O. |
author_sort |
Zielinski, S. |
title |
Temperature Effects on Hemocyanin Oxygen Binding in an Antarctic Cephalopod |
title_short |
Temperature Effects on Hemocyanin Oxygen Binding in an Antarctic Cephalopod |
title_full |
Temperature Effects on Hemocyanin Oxygen Binding in an Antarctic Cephalopod |
title_fullStr |
Temperature Effects on Hemocyanin Oxygen Binding in an Antarctic Cephalopod |
title_full_unstemmed |
Temperature Effects on Hemocyanin Oxygen Binding in an Antarctic Cephalopod |
title_sort |
temperature effects on hemocyanin oxygen binding in an antarctic cephalopod |
publisher |
University of Chicago Pr. |
publishDate |
2001 |
url |
https://oceanrep.geomar.de/id/eprint/53044/ https://oceanrep.geomar.de/id/eprint/53044/1/3744.pdf https://www.journals.uchicago.edu/doi/abs/10.2307/1543086 https://doi.org/10.2307/1543086 |
geographic |
Antarctic The Antarctic |
geographic_facet |
Antarctic The Antarctic |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_relation |
https://oceanrep.geomar.de/id/eprint/53044/1/3744.pdf Zielinski, S., Sartoris, F. J. and Pörtner, H. O. (2001) Temperature Effects on Hemocyanin Oxygen Binding in an Antarctic Cephalopod. Open Access The Biological Bulletin, 200 (1). pp. 67-76. DOI 10.2307/1543086 <https://doi.org/10.2307/1543086>. doi:10.2307/1543086 |
op_rights |
info:eu-repo/semantics/openAccess |
op_doi |
https://doi.org/10.2307/1543086 |
container_title |
The Biological Bulletin |
container_volume |
200 |
container_issue |
1 |
container_start_page |
67 |
op_container_end_page |
76 |
_version_ |
1766142748388229120 |