guanosine-triphosphate and demethylchlordimeform

3H-Octopamine binds reversibly and with high affinity to sites on adult firefly light organ membranes. The binding is characterized by multiple affinities. Scatchard analysis supported a two site binding model with a tentative Kd value of about 1 nM for the high affinity component. The more abundant lower affinity site had a Kd value of about 60 nM. Guanyl nucleotides (Gpp(NH)p and GTP) greatly reduced the apparent number of octopamine binding sites. Competition studies with known octopaminergic agonists including the formamidine pesticides chlordimeform (CDM) and N-demethyl chlordimeform (DCDM) showed the following rank order of potencies in displacing octopamine: DCDM greater than octopamine = synephrine greater than naphazoline greater than clonidine greater than CDM. It was also observed that phentolamine was much more active than propranolol in antagonizing OA-binding. These relative activities are similar to the abilities of the same compounds to alter adenylate cyclase activity in light organ homogenates. Together with the effect of GTP on binding, these results suggest that the binding sites are functional octopamine receptors of the light organ.

Topics: Animals; Binding Sites; Binding, Competitive; Chlorphenamidine; Clonidine; Coleoptera; Guanosine Triphosphate; Male; Naphazoline; Octopamine; Phentolamine; Propranolol; Receptors, Adrenergic; Receptors, Biogenic Amine; Synephrine