Abstract
At a pH around 7.5 with 0.05 M NaP i, the shape of the oxygen equilibrium curve of hemoglobin from the bluefin tuna ( Thunnus thynnus) is temperature dependent. The affinity at low saturation increases, and that at high saturation decreases on cooling from 20°C to 10°C. The equilibrium curves at the two temperatures therefore cross over. This behavior is physiologically advantageous to a warm-bodied fish. It may be explained in terms of the two-state model by supposing that the allosteric constant L increases markedly on cooling the solutions.
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