Journal article
Whole blood-oxygen binding properties of four cold-temperate marine fishes: blood affinity is independent of pH-dependent binding, routine swimming performance, and environmental hypoxia
Marine Biological Laboratory, University of Copenhagen, Strandpromenaden 5, DK-3000 Helsingør, Denmark. n.herbert@bio.gla.ac.uk1
The relationship between whole blood-oxygen affinity (P(50)) and pH-dependent binding (i.e., cooperativity and the Bohr [ Phi ] and Root effects) was examined statistically under standardized conditions (10.0 degrees Celsius) 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>plaice>mackerel>cod), and this was independent of both swimming performance and the predicted low O(2) 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 ( Phi 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.
Language: | English |
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Publisher: | The University of Chicago Press |
Year: | 2006 |
Pages: | 909-18 |
ISSN: | 15375293 and 15222152 |
Types: | Journal article |
DOI: | 10.1086/506000 |
ORCIDs: | Steffensen, John F |