Acetylcholine receptor binding site contains a disulfide cross-link between adjacent half-cystinyl residues.

@article{Kao1986AcetylcholineRB,
  title={Acetylcholine receptor binding site contains a disulfide cross-link between adjacent half-cystinyl residues.},
  author={Peter N Kao and A. Karlin},
  journal={The Journal of biological chemistry},
  year={1986},
  volume={261 18},
  pages={8085-8}
}
A conserved feature of all nicotinic receptors is the presence of a readily reducible disulfide bond adjacent to the acetylcholine binding site. Previously we showed that in intact receptor from Torpedo californica electric tissue reduction of this disulfide followed by affinity alkylation with 4-(N-maleimido)benzyltri[3H] methylammonium iodide specifically and uniquely labels the alpha subunit residues Cys-192 and Cys-193. To identify all of the half-cystinyl residues contributing to the… CONTINUE READING

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