High-affinity binding of crustacean hyperglycemic hormone (CHH) to hepatopancreatic plasma membranes of the crab Carcinus maenas and the crayfish Orconectes limosus.

The binding properties of the crustacean hyperglycemic hormone (CHH) of two species, the shore crab, Carcinus maenas (Brachyura) and the crayfish, Orconectes limosus (Astacura), were investigated using purified plasma membranes of one of the main target organs, the hepatopancreas. Assays were performed under equilibrium binding conditions with 125I-CHH as labeled ligand and unlabeled CHH in increasing concentrations as displacing ligand. In both cases, comparable binding characteristics were observed for the homologous CHH to the respective hepatopancreatic membrane source, indicating saturable and displaceable binding with nonlinear dependence on monovalent cations and a dissociation constant (Kd) of 4 to 6 x 10(-10) M. Binding capacity was in the range of 200-400 fmol/mg membrane protein. In heterologous displacement studies a certain degree of species specificity was found, particularly with regard to selective binding by the Orconectes receptor, suggesting that the group specificity of biological activity of CHH reflects coevolution of both hormone and receptor.