Structure and Characterization of the Ion-Channel of the Nicotinic Acetylcholine Receptor

Abstract

The nicotinic acetylcholine receptor (AcChR) is a complex of four polypeptides of molecular weight 40,000, 50,000, 60,000 and 65,000 daltons, generally referred to as alpha, Beta, gamma, sigma, which we first described (1) and this has since been confirmed in several laboratories (2). By performing amino-terminal amino acid sequence analysis of these four polypeptides we demonstrated that they are a highly homologous set of proteins (3) presumably derived from a single ancestral gene and further that they are associated with a stoichiometry of alpha, Beta, gamma, sigma in AcChR from the electric ray, Torpedo californica, the most convenient source of this receptor molecule. Based on the amino acid sequence data we obtained, four groups constructed nucleotide probes for the isolation of C-DNA for subsequent sequence determination. (kt)

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Document Details

Document Type
Technical Report
Publication Date
Jul 01, 1984
Accession Number
ADA218380

Entities

People

  • Michael A. Raftery

Organizations

  • California Institute of Technology

Tags

Communities of Interest

  • Biomedical

DTIC Thesaurus Topics

  • Amides
  • Amino Acids
  • Animal Structures
  • Biochemistry
  • Central Nervous System
  • Chemical Reactions
  • Chemistry
  • Cholesterol
  • Classification
  • Controlled Atmospheres
  • Fish
  • Gel Electrophoresis
  • Identification
  • Membrane Lipids
  • Membrane Proteins
  • Protein Sequence Analysis
  • Sequence Analysis

Fields of Study

  • Biology

Readers

  • Molecular and Cellular Biochemistry
  • Solar Physics