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.

• Published in: Physiological and Biochemical Zoology
• Main Authors: Herbert, Neill A, Skov, Peter V, Wells, Rufus M G, Steffensen, John F
• Format: Article in Journal/Newspaper
• Language: English
• Published: 2006
• Subjects: Gadus morhua
• Online Access: https://curis.ku.dk/portal/da/publications/whole-bloodoxygen-binding-properties-of-four-coldtemperate-marine-fishes-blood-affinity-is-independent-of-phdependent-binding-routine-swimming-performance-and-environmental-hypoxia(d5150f20-384c-11dd-b7b4-000ea68e967b).html; https://doi.org/10.1086/506000

Udgivelsesdato: null-null 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.