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.

TY - JOUR

T1 - 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.

AU - Herbert, Neill A

AU - Skov, Peter V

AU - Wells, Rufus M G

AU - Steffensen, John F

N1 - Keywords: Animals; Cold; Ecosystem; Fishes; Hydrogen-Ion Concentration; Oceans and Seas; Oxygen; Swimming

PY - 2006

Y1 - 2006

N2 - 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.

AB - 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.

U2 - 10.1086/506000

DO - 10.1086/506000

M3 - Journal article

C2 - 16927237

SN - 1522-2152

VL - 79

SP - 909

EP - 918

JO - Physiological and Biochemical Zoology

JF - Physiological and Biochemical Zoology

IS - 5

ER -