The thermal sensitivity of oxygen binding has been studied at 10, 15, 20 and 25 °C in whole blood from specimens of Neptunea antiqua acclimated to ambient salinities of 24 and 35 ‰. The O2 affinity is strongly pH-dependent, demonstrating a large reversed Bohr shift below pH 8.0. The magnitude of the Bohr shift is not significantly influenced by temperature or ionic concentration. At 35 ‰, the blood O2-affinity is strongly influenced by temperature (ΔHapp≈ −58.6 kJ mol−1), while at 24 ‰ there is almost no temperature sensitivity (ΔHapp<−18.8 kJ mol−1).

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