Specific binding properties of 125I-apamin in various structures of the rat central nervous system.

The properties of 125I-apamin binding with rat central nervous system slices were analysed in vitro using computerized densitometric autoradiography. Scatchard analysis performed for the data of binding experiments in rat brain and spinal cord demonstrates that apamin binds to a single class of non-interacting binding sites in all investigated structures. The dissociation constant values (KD) were similar in all investigated structures (31-38 pM). The maximal binding capacity (Bmax) was observed in the structures of limbic olfactory system (30 fmol/mg protein), the lowest in brain white matter (0.5 fmol/mg protein). It is concluded that the observed pattern of 125I-apamin binding might represent the topography of a class of Ca2+ dependent K+ channels in the rat central nervous system.