Abstract
Crayfish, Pacifastacus leniusculus, were acclimated to 10, 20, and 25 degrees C for 1 mo. Hemocyanin from animals at these three acclimation temperatures showed distinctly different oxygen binding patterns. At any particular set of test temperature and pH, hemocyanin from 10 degrees C-acclimated animals had the lowest oxygen affinity and the greatest cooperativity, whereas hemocyanin from 25 degrees C-acclimated animals had the highest oxygen affinity and the lowest cooperativity. When tested at their own acclimation temperature, and at normal hemolymph pH for that temperature, all three hemocyanins showed oxygen pressure for half-saturation of hemoglobin of 6-7 Torr. Thus acclimation keeps oxygen affinity centered around a narrow range of values. The acclimation response probably eliminates hemocyanin oxygen affinity as a major factor in the decline of oxygen uptake ability in the crayfish above 20 degrees C. The structural basis for the observed functional changes in the hemocyanin is not yet clear.
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