The regulation of whole blood oxygen affinity in the freshwater blackfish Gadopsis marmoratus Richardson has been examined, and correlations made between oxygen-binding properties and the habitat and swimming behaviour of the fish.
Blackfish whole blood has a low oxygen affinity relative to other fish bloods reported in the literature. This is not due to a low oxygen affinity of the stripped haemoglobins, but arises from interactions between haemoglobin and intraerythrocytic modulators.
The presence of high concentrations of ATP, and to a lesser extent GTP, in the erythrocyte, together with the effect of these nucleoside triphosphates on the oxygen affinity of haemoglobin solutions at physiological NTP: Hb4 molar ratios, demonstrates that this class of compounds is a major regulator of oxygen affinity in blackfish blood.
The oxygen affinities of whole blood and haemoglobin solutions are sensitive to pH, with haemoglobin solutions displaying a relatively large alkaline Bohr coefficient of - 1.05 over the physiologically relevant pH range of 6.5–7.0.
Although increasing Pco2, lowers the oxygen affinity of whole blood, it does so only through the effect on pH, as pH-buffered haemoglobin solutions show no oxygen-linked CO2 binding. This lack of oxygen-linked CO2 binding has not been reported for any other naturally occurring vertebrate haemoglobins.
Muscle morphology and biochemistry, and behavioural observations, indicate that the blackfish uses anaerobic energy metabolism during rapid swimming and in recovery.
It is concluded that the oxygen-binding properties of blackfish blood reflect adaptations for maintaining adequate tissue oxygenation for animals at rest and during slow sustained swimming in waters of high oxygen tensions.
Regulation of Blood Oxygen Affinity in the Australian Blackfish Gadopsis Marmoratus: I. Correlations between Oxygen-binding Properties, Habitat and Swimming Behaviour
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G. P. DOBSON, J. BALDWIN; Regulation of Blood Oxygen Affinity in the Australian Blackfish Gadopsis Marmoratus: I. Correlations between Oxygen-binding Properties, Habitat and Swimming Behaviour. J Exp Biol 1 August 1982; 99 (1): 223–243. doi: https://doi.org/10.1242/jeb.99.1.223
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