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Oxygenation properties of haemoglobins from the flatfish plaice (Pleuronectes platessa) and flounder (Platichthys flesus)

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Summary

The oxygen binding properties and some haematological data of haemoglobins of plaice (Pleuronectes platessa) and flounder (Platichthys flesus) were measured and compared, with the view of discerning their adaptations to the benthic habitat.

Compared to plaice, flounders posses higher haematocrit and haemoglobin levels, and their haemoglobin has a higher oxygen affinity, smaller Bohr and Root effects and appears to have a greater ATP sensitivity. At pH 7.6, the half-saturation oxygen tensions,P 50, of stripped plaice and flounder haemoglobins amount to about 5.9 and 4.2 torr, and the Bohr shifts (ΔlogP 50/Δ pH) to −0.51 and −0.34, respectively. The species differences in the oxygen binding patterns occur after stripping the haemoglobin in solution, from dissolved ions and thus appear to be inherent in the pigment molecules. The differences suggest that the haemoglobin of flounder is better adapted to hypoxic and hypercarbic environments than plaice haemoglobin, in accordance with the more inshore occurrence of the former species.

The molar ratios of ATP to haemoglobin tetramers are low in plaice and flounder (about 1.6); in plaice this ratio corresponds to that where the cofactor effect is most pronounced. In contrast to previous evidence for an adaptive reduction in the temperature dependence of the haemoglobin of flounder but not of plaice from the Baltic Sea (Friedrich, 1935), the same temperature effects were found in representatives of the two species both from the Dutch North Sea and the Danish Kattegat.

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Weber, R.E., de Wilde, J.A.M. Oxygenation properties of haemoglobins from the flatfish plaice (Pleuronectes platessa) and flounder (Platichthys flesus). J Comp Physiol B 101, 99–110 (1975). https://doi.org/10.1007/BF00694151

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