Abstract
AbstractThe oxygen affinity of the blood of the hermit crab Pagurus bernhardus is temperature independent at constant physiological pH (7.8 to 8.0) reflecting zero overall heat of oxygenation under these conditions. Combined with the absence of an indirect temperature effect (via changed in vivo pH), this represents a unique situation compared with previously investigated hemocyanins, and reflects adaptations to stabilize hemocyanin O2 loading in the thermolabile natural environments.
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