TY - JOUR
T1 - Mapping of the polypeptide chain organization of the main extracellular domain of the α-subunit in membrane-bound acetylcholine receptor by antipeptide antibodies spanning the entire domain
AU - Atassi, M. Z.
AU - Mulac-Jericevic, B.
AU - Ashizawa, T.
N1 - Copyright:
Copyright 2020 Elsevier B.V., All rights reserved.
PY - 1994
Y1 - 1994
N2 - To study the organization of the polypeptide chain of the main extracellular domain of the nicotinic acetylcholine receptor (AChR) α- subunit, we examined the ability of the native membrane-bound AChR of Torpedo californica (T-AChR) to bind a panel of antibodies against overlapping synthetic peptides which collectively encompassed this entire domain. Antibodies against the α-chain peptides α1-16, α89-104 and α158-174 were able to bind to membrane-bound T-AChR. Other anti-peptide antibodies showed little or no binding to T-AChR in the membrane. It is concluded that regions α1-16, α89-104 and α158-174 are highly exposed on the surface of the α subunit of membrane-bound AChR.
AB - To study the organization of the polypeptide chain of the main extracellular domain of the nicotinic acetylcholine receptor (AChR) α- subunit, we examined the ability of the native membrane-bound AChR of Torpedo californica (T-AChR) to bind a panel of antibodies against overlapping synthetic peptides which collectively encompassed this entire domain. Antibodies against the α-chain peptides α1-16, α89-104 and α158-174 were able to bind to membrane-bound T-AChR. Other anti-peptide antibodies showed little or no binding to T-AChR in the membrane. It is concluded that regions α1-16, α89-104 and α158-174 are highly exposed on the surface of the α subunit of membrane-bound AChR.
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U2 - 10.1007/978-1-4615-2427-4_19
DO - 10.1007/978-1-4615-2427-4_19
M3 - Article
C2 - 7526636
AN - SCOPUS:0028246998
SN - 0065-2598
VL - 347
SP - 221
EP - 228
JO - Advances in experimental medicine and biology
JF - Advances in experimental medicine and biology
ER -