Structure and function of the hemocyanin from a semi-terrestrial crab, Ocypode quadrata.

Structural and functional studies of the hemocyanin of the semi-terrestrial ghost crab, Ocypode quadrata, demonstrate a variety of differences in comparison to the hemocyanin of aquatic crabs. These differences may be related to the terrestrial habit of this crab. Unlike aquatic crabs, the major (56%) blood component is the hexamer; the remaining 44% is dodecamer. The hexamers and dodecamers are not in rapid equilibrium. Electrophoretic analysis of the subunit composition indicates three major components referred to as 1, 3, and 4, and one minor component referred to as component 2. These components, although electrophoretically distinct, are alike immunologically. Components 1 and 2 are essentially absent from purified hexamers, whereas they compose 1/3 of the subunits in dodecamers. These results suggest that they are involved in linking hexamers to form dodecamers, and that two, rather than one, subunits are involved in the bridge. Oxygen-binding measurements show a higher degree of cooperativity, and a much reduced allosteric effect of L-lactate on the dialyzed hemocyanin as compared to the hemocyanin of aquatic crabs. Exercise rapidly induces a large drop in hemolymph pH (0.5 units) and a corresponding increase in lactate concentrations (to 10 mM).