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

M. Z. Atassi, B. Mulac-Jericevic, T. Ashizawa

Research output: Contribution to journalArticle

4 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)221-228
Number of pages8
JournalAdvances in experimental medicine and biology
Volume347
DOIs
StatePublished - 1994

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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