The isolation and characterisation of the nicotinic acetylcholine receptor from human skeletal muscle.

@article{Stephenson1981TheIA,
  title={The isolation and characterisation of the nicotinic acetylcholine receptor from human skeletal muscle.},
  author={F Anne Stephenson and R{\'o}ger Churnside Harrison and G. G. Lunt},
  journal={European journal of biochemistry},
  year={1981},
  volume={115 1},
  pages={
          91-7
        }
}
Nicotinic acetylcholine receptor protein has been purified from human skeletal muscle by a procedure involving extraction in non-ionic detergent followed by affinity purification on immobilised alpha-toxin. Purified receptor preparations had specific activities of 0.5-3.5 mumol alpha-bungarotoxin binding sites/g protein and sedimented as a single 125I-alpha-bungarotoxin-binding species in sucrose-density-gradient centrifugation with s20,w = 9.5 S. The purified protein focussed as a single sharp… CONTINUE READING
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