scholarly journals Effect of local anaesthetics on steroid-nicotinic acetylcholine receptor interactions in native membranes of Torpedo marmorata electric organ

1990 ◽  
Vol 1027 (3) ◽  
pp. 287-294 ◽  
Author(s):  
H.R. Arias ◽  
M.B. Sankaram ◽  
D. Marsh ◽  
F.J. Barrantes
Keyword(s):  
Acetylcholine Receptor ◽  
Nicotinic Acetylcholine Receptor ◽  
Electric Organ ◽  
Local Anaesthetics ◽  
Torpedo Marmorata ◽  
Nicotinic Acetylcholine ◽  
Receptor Interactions

scholarly journals Synthesis of an antigenic site of native acetylcholine receptor peptide 159-169 of Torpedo acetylcholine receptor α-chain

1985 ◽  
Vol 226 (1) ◽  
pp. 193-197 ◽  
Author(s):  
D J McCormick ◽  
V A Lennon ◽  
M Z Atassi
Keyword(s):  
Acetylcholine Receptor ◽  
Nicotinic Acetylcholine Receptor ◽  
Antigenic Site ◽  
Electric Organ ◽  
Alpha Subunit ◽  
Nicotinic Acetylcholine ◽  
Antigenic Region ◽  
Torpedo Electric Organ ◽  
Α Chain ◽  
Immobilized Peptide

A region of the alpha-subunit of the nicotinic acetylcholine receptor (AChR) of the Torpedo electric organ, containing residues 161-166, has been proposed to be a major antigenic site in the native AChR protein. We report the synthesis of a peptide corresponding to residues 159-169, which contains the proposed antigenic region. In quantitative radiometric titrations, radiolabelled anti-(native AChR) antibodies from three different species, rabbit, rat and dog, exhibited considerable binding (approx. 15% relative to native AChR) to Sepharose-immobilized peptide 159-169, but did not bind significantly to Sepharose-immobilized unrelated proteins or peptides. Specificity was further confirmed by the finding that no rabbit anti-AChR antibodies bound to the peptide after absorption with native AChR. These data indicate that the region 159-169 contains an antigenic site that is readily accessible in solubilized native Torpedo AChR.

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