Abstract
Characteristics of specific125I-omega-conotoxin (ω-CgTX) binding were systematically investigated in crude membranes from rat whole brain. Kd and Bmax Values for the binding were 49.7 pM and 181.5 fmol/mg of protein, respectively. The effects of various types of Ca channel antagonists on the binding were investigated. Dynorphin A (1–13), in particular, specifically inhibited125I-ω-CgTX binding, but not that of [3H](+)PN200-110. Spider venom fromPlectreurys tristes did not specifically inhibit specific binding of125I-ω-CgTX, because the venom also inhibited the binding of [3H](+)PN200-110 to a similar degree. The amount of specific binding of125I-ω-CgTX was less in the cerebellum than that in any other area of whole brain. The cross-linker disuccinimidyl suberate did not label with125I-ω-CgTX and its binding sites in rat whole brain, although it did in chick whole brain, which was used as a positive control. These findings suggested that dynorphine A (1–13) was a selective blocker of ω-CgTX-sensitive Ca channels in crude membranes from rat whole brain and that ω-CgTX-sensitive Ca channels were mainly present a rat brain except cerebellum.
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Ichida, S., Wada, T., Sekiguchi, M. et al. Characteristics of specific125I-ω-conotoxin GVIA binding in rat whole brain. Neurochem Res 18, 1137–1144 (1993). https://doi.org/10.1007/BF00978364
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DOI: https://doi.org/10.1007/BF00978364