Affinity of cholinergic ligands for the partially purified acetylcholine receptor from mammalian skeletal muscle

Dolly, J. Oliver; Barnard, Eric A.

doi:10.1016/0014-5793(74)80355-8

Cited by 17 publications

(2 citation statements)

References 13 publications

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“…Muscles, denervated 3-4 weeks, were removed as noted from cats, rabbits or rats. Labelling of the receptor, and its assay (Dolly & Barnard, 1974), used its specific reaction with [3H]a-neurotoxin (Barnard et a/., 1971), in this case an a-neurotoxin from Naja melanoleuca venom, labelled at 5.7-1 8 Ci/mmol by catalytic halogen-exchange tritiation at a single histidine carbon (A. Menez, E. A. Barnard, J. 0.…”

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confidence: 99%

Size and Molecular Properties of the Acetylcholine-Receptor Protein of Muscle

Barnard

Dolly

et al. 1978

Biochemical Society Transactions

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ligand because the smaller molecular forms, which would be better able to penetrate the agarose gel, are not bound, whereas the larger form does bind. The gel can also discriminate between acetylcholinesterase and cholinesterase. This is unexpected because edrophonium is a competitive inhibitor of both enzymes. This suggests that the coupling of a side chain to the meta-hydroxy group of edrophonium alters the inhibitory properties of the molecule.

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Size and Molecular Properties of the Acetylcholine-Receptor Protein of Muscle

Barnard

Dolly

et al. 1978

Biochemical Society Transactions

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“…This form of the ACh.R has recently been partially purified from cat denervated leg muscles, and shown to bind cholinergic agonists and antagonists with high affinities (Dolly and Barnard, 1974;Barnard et al, 1975). It has also recently been partly purified from denervated and innervated rat muscle (Brockes and Hall, 1975; Almon and Appel, 1976a).…”

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confidence: 99%