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- W87591090 abstract "Publisher Summary This chapter describes the structure of nicotinic acetylcholine (ACh) receptors. The nicotinic ACh receptor has been extracted and purified to homogeneity from various electroplaque and muscle sources, the pure protein always having a specific binding activity for post-synaptic α-toxins of 8000–10,000 nmoles/g protein. By the analysis of sodium dodecyl sulfate (SDS) gels, the pure Torpedo ACh receptor has the subunit structure of α2βγδ (in order of increasing size) and the pure cat muscle receptor has only 43,000 MW subunits. Each appears to have two α subunits per 9 S molecule. The other subunits in the cat muscle receptor are of the same size at the α-subunit but differ from it in certain respects. Muscle ACh receptors from some other species have at least one heavier subunit in addition; therefore, the composition of the molecule varies considerably between sources. In the muscles of 4 vertebrate species tested, the α-subunit is always the major one; its exact molecular weight varies in each species but is always 40–43,000. The α-subunits of different species can be separated by lowering the cross-linking reagent concentration in the polyacrylamide gels." @default.
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- W87591090 date "1980-01-01" @default.
- W87591090 modified "2023-09-23" @default.
- W87591090 title "CURRENT VIEWS ON THE STRUCTURE OF NICOTINIC ACETYLCHOLINE RECEPTORS FROM DIFFERENT SOURCES" @default.
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- W87591090 doi "https://doi.org/10.1016/b978-0-08-025921-5.50045-x" @default.
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