By Kimon J. Angelides (auth.), Toshio Narahashi (eds.)
A wealth of data has been amassed concerning the functionality of ion channels of excitable cells because the vast and pioneering voltage clamp stories by means of Hodgkin, Huxley, and Katz 36 years in the past. The research of ion chan nels has now reached a degree at which a quantum leap in growth is antici pated. there are lots of solid purposes for this. Patch clamp innovations origi nally constructed by way of Neher and Sakmann 12 years in the past have made it attainable to review the functionality of ion channels in numerous cells. Membrane ionic currents can now be recorded virtually from many sorts of cells utilizing the whole-cell patch clamp process. the hole and shutting of person ion channels might be analyzed utilizing the single-channel patch clamp approach. ideas have additionally been built to include purified ion channels into lipid bilayers to reconstitute an "excitable membrane. " complicated tech niques constructed in molecular biology, genetics, and immunology, similar to gene cloning and using monoclonal antibodies, at the moment are being utilized to the examine of ion channels. quite a few medicinal drugs have now been came across or are suspected to have interaction with ion channels to exert healing results. as well as the classical examination ples, as represented by way of neighborhood anesthetics, many different medications, together with cal cium antagonists, psychoactive medicinal drugs, cardiac medicines, and anticonvulsants, proven to change ion channel functionality. For sure insecticides resembling were pyrethroids and DDT, sodium channels are sincerely the most important aim site.
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Additional resources for Ion Channels: Volume 1
Sample text
These segments, according to the model of Guy and Seetharlamu (1986) are postulated to be short, partially amphipathic a-helices with some negative side chains. The S4 segment is a highly arginine-rich peptide which is found in 'each of the four domains of the channel and is thought to represent the FLUORESCENCE SPECTROSCOPY 35 TTx BTx o I- 40A ·1 Css Site Domain C, 57 Residues 1220-1239 C FIGURE 10. Molecular model of the voltage-dependent Na + channel from fluorescence energy transfer measurements and protein biochemical data.
3). 4. , 1984). We have utilized this information after covalent cross-linking of the scorpion toxin derivatives to specific peptides of the channel. The Denny-Jaffe reagent N-4-( 4' -azido-3' -125I-iodophenylazo )-benzoyl3-aminopropyl-N-oxy succinimide ester, which is a photoactivatable, heterobifunctional, cleavable, 125I-Iabeled cross-linking agent, was coupled to the scorpion toxins via the activated ester portion. Membranes enriched for Na + channels were obtained from electric eel and the 260,OOO-dalton peptide of the channel was specifically labeled.
Equilibrium binding measurements could not resolve these subtle interactions although there is some electrophysiological evidence supporting the idea that these toxin sites interact on the channel. The fluorescence measurements were the first direct indication of this subtle conformational coupling between these separate receptor sites. In the absence of other ligands, the fluorescence emission of Css indicates that the (3-scorpion toxin binding site is largely hydrophobic, like that of the a-scorpion toxin receptor.
