Specific binding of perhydrohistrionicotoxin to Torpedo acetylcholine receptor.
- 1 June 1979
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 76 (6) , 2576-2579
- https://doi.org/10.1073/pnas.76.6.2576
Abstract
T. californica postsynaptic membrane fragments were treated with base, which resulted in membranes that were depleted of many nonacetylcholine receptor polypeptides and contained acetylcholine receptor subunits of Mr [MW ratio] 40,000, 50,000, 60,000 and 65,000 (Raftery et al., (1975)). A 43,000 Mr polypeptide and some other components were quantitatively extracted. Base-treated membranes retained the capacity to bind [3H]perhydrohistrionicotoxin and the local anesthetics dibucaine and tetracaine. The regulation of this binding by carbamylcholine, and the kinetic mechanism of perhydrohistrionicotoxin binding, was unchanged. [3H]Perhydrohistrionicotoxin binding activity was largely reconstituted from 2% sodium cholate extracts of base-treated membranes. The perhydrohistrionicotoxin binding site appears to be located on 1 or more of the acetylcholine receptor polypeptides, and the reconstitution of that binding site from detergent extracts does not require the presence of a 43,000 Mr polypeptide.This publication has 20 references indexed in Scilit:
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