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1 Department of Biology, College of William and Mary, Williamsburg, VA 23185
2 Marine Biomedical Center, Duke University Marine Laboratory, Beaufort, NC 28516
The effects of salinity changes on the oxygen binding properties of hemocyanin have been examined in the blue crab Callinectes sapidus. Oxygen affinity increases measurably with increases in Ca+2, Mg+2 or Na+ but, within the physiological range, not K+. Unlike its large and specific influence on other arthropod hemocyanins, Cl- has little or no effect. Ca+2, alone and in physiological concentrations, restores oxygen affinity to the level observed in a complete physiological saline. Ca+2 also restores the Bohr shift to the physiological level. Physiological variation in inorganic ions (or pH) does not affect the cooperativity of oxygen binding.
Physiological variation in Ca+2 explains only a minor fraction of the actual change in oxygen affinity that accompanies acclimation to a new salinity. The aclimation, which occurs within 8 days, requires a non-dialyzable factor in the blood. The non-dialyzability of the factor and the previous reports of a large increase in blood protein levels at low salinity might implicate an intrinsic change in the hemocyanin molecule with salinity, a suggestion that is also supported by apparent differences in the subunit composition of the molecule in the high and low salinity acclimated crabs. Using paired observations on the same individuals before and after acclimation, however, we were able to demonstrate relatively small changes in hemocyanin concentration. Moreover, the relationship between the differences in subunit composition and HcO2 binding is uncertain. The identity of the factor remains unknown.
Submitted on August 9, 1982
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