Haemocyanin oxygen binding and the physiological ecology of a range of talitroidean amphipods (Crustacea) I. pH, temperature, and l-lactate sensitivity

Abstract

The effect of pH, temperature, and l-lactate on the O2 bindign properties of haemocyanin (Hc) from three talitroidean species i.e., the aquatic Apohyale pugettensis, the semi-terrestrial Megalorchestia californiana, and the semi-/euterrestrial Traskorchestia traskiana was studied. The Hc of A. pugettensis was characterized by a higher O2 affinity (and more pronounced Bohr shift) than the Hc of either M. californiana or T. traskiana. Apohyale was the only species that possessed He that was sensitive to temperature change. Resuspending Hc from each of the three species in a stock Ringer's solution (based on the ionic composition of the haemolymph of T. traskiana) showed that the persistence of the difference in Bohr shift between Apohyale and the other two species was due to differences in the haemocyanins themselves and not attributable to their respective ionic environments. An inverse relationship was found between the cooperativity (n50) and pH of Hc from T. traskiana and A. pugettensis but not for M. californiana. In each case adding l-lactate increased Hc O2 affinity, but this was most pronounced for A. pugettensis.