Janicki, P. K.: Specific binding properties of ¹²⁵ I-apamin to various structures of the rat central nervous system. Acta physiol, pol., 1989, 40 (2): 235-239. The properties of ¹²⁵ I-apamin binding with raft ceaxtrail 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) weTe 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 ¹²⁵ I-apamin binding might represent the topography of a class of Ca²⁺ dependent K⁺ channels in the rat central nervous system.
Janicki, P. K., Seibold, G., Siembab, D., Paulo, E. A., and Szreniawski, Z.: Computer assisted quantitative densitometric analysis of ¹²⁵ I-apamin binding sites in the central nervous system. Acta physiol, pol., 1989, 40 (2): 240-249. The binding sites for ¹²⁵ I-monoiododerivative of apamin in the central nervous system of rat, guinea-pig, Chicken and frog were analysed and compared by computer assisted quantitative densitometric autoradiography on X-ray film. The highest level of binding sites in the rat and guinea-pig brain was found in the limbic-olfactoTy system and in the substantia gelatinosa of the spinal cord. In the chicken brain apamin binds preferentially to the tectum opticum and nuclei isthmi. In the frog brain no specific apamin binding sites were found. The role of presented topography for apamin binding sites is discussed in relation to neurotoxic properties of apamin.
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