Whole Blood–Oxygen Binding Properties of Four Cold-Temperate Marine Fishes: Blood Affinity Is Independent of pH-Dependent Binding, Routine Swimming Performance, and Environmental
The relationship between whole blood–oxygen affinity (P50) and pH-dependent binding (i.e., cooperativity and the Bohr [F] and Root effects) was examined statistically under standardized conditions (10.0�C) in four unrelated cold-temperate marine fishes that differ widely in their swimming performanc...
| Main Authors: | , , , |
|---|---|
| Other Authors: | |
| Format: | Text |
| Language: | English |
| Subjects: | |
| Online Access: | http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.139.9446 http://www.mbl.ku.dk/JFSteffensen/PhysBiochemZool%202006.pdf |
| Summary: | The relationship between whole blood–oxygen affinity (P50) and pH-dependent binding (i.e., cooperativity and the Bohr [F] and Root effects) was examined statistically under standardized conditions (10.0�C) in four unrelated cold-temperate marine fishes that differ widely in their swimming performance and their expected responses to hypoxia: cod (Gadus morhua), herring (Clupea harengus), mackerel (Scomber scombrus), and plaice (Pleuronectes platessa). An unexpected difference in blood-oxygen affinity was found (herring 1 plaice 1 mackerel 1 cod), and this was independent of both swimming performance and the predicted low O2 response of each species. The ecotype of the four marine species was also unrelated to pH-dependent binding because no difference in the Bohr effect was apparent (F varied insignificantly from �0.90 to �1.06), and differences in the magnitude of the cooperative binding reaction were associated only with the presence of the Root effect. Although several reviews propose a generalized link between blood-oxygen affinity and pH-dependent binding, our results advise against overestimating the adaptive functional properties of hemoglobin across unrelated species. |
|---|