Abstract
The distinct molecular identities of ionic channels within biological membranes are now being revealed. The acetylcholine receptor, a ligandgated cation channel, was solubilized and purified from post-synaptic membranes of the ray Torpedo californica (Karlin, 1980; Changeux, 1981). Entire amino acid sequences for all of the acetylcholine receptor subunits were deduced from DNA sequence analysis of cDNA clones (Numa et al., 1983). Similarly, the voltage-sensitive Na+ channel from rat brain has been solubilized and purified to homogeneity, and shown to consist of α (Mr 260,000), β1 and β2(Mr 39,000 and 37,000, respectively) subunits (Agnew et al., 1980; Weigele and Barchi, 1982; Hartshorne and Catterall, 1984). Consistent with the heterogeneity of tetrodotoxin binding sites, presence of at least three distinct Na+ channels (I, II and III) in rat brain was suggested from a sequencing study of cDNA clones obtained from three distinct mRNAs for the α-subunit (Noda et al., 1986). The Ca2+ channel (a dihydropyridine-sensitive class) was also purified (Curtis and Catterall, 1985). None of the known K+ channels have yet been purified, probably due to the unavailability of high affinity neurotoxins and a K+ channel abundance which is small in comparison to that of the Na+ channel and the acetylcholine receptor.
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Alkon, D.L., Naito, S. (1987). Long-Term Synergistic Regulation of Ionic Channels by C-Kinase and Ca2+/CaM-Type II Kinase. In: Ehrlich, Y.H., Lenox, R.H., Kornecki, E., Berry, W.O. (eds) Molecular Mechanisms of Neuronal Responsiveness. Advances in Experimental Medicine and Biology, vol 221. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-7618-7_20
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DOI: https://doi.org/10.1007/978-1-4684-7618-7_20
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