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Title: Characterization of a putative acetylcholine receptor in chick ciliary ganglion neurons

Abstract

Monoclonal antibodies to the main immunogenic region on the alpha subunit of acetylcholine receptors in muscle and electric organ recognize membrane components in chick brain and ciliary ganglia that are candidates for the neuronal receptor. The component in chick brain has been purified by immunoaffinity chromatography. It specifically binds nicotine but not alpha-bungarotoxin, and can be affinity labeled with (/sup 3/H)bromoacetylcholine. The cross-reacting component in ciliary ganglion neurons is concentrated in synaptic membrane, and can be modulated by exposure of the cells to cholinergic ligands in culture. The cross-reacting component in ciliary ganglion neurons is an integral membrane component that binds concanavalin A, and it is distinct from the alpha-bungarotoxin binding component. The acetylcholine receptor function in these neurons can be locked by affinity alkylation with bromoacetylcholine, indicating similarity in this respect to receptors from muscle and electric organ. Antisera raised against the partially purified component from chick brain also block receptor function on ciliary ganglion neurons. The subcellular distribution of the ganglion component in culture is assessed, and it is shown that approximately 2/3 of the cross-reacting components are intracellular; the majority of these seem not to be destined for insertion into the plasma membrane.

Authors:
Publication Date:
Research Org.:
California Univ., San Diego (USA)
OSTI Identifier:
5219891
Resource Type:
Thesis/Dissertation
Resource Relation:
Other Information: Thesis (Ph. D.)
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; ACETYLCHOLINE; BIOCHEMICAL REACTION KINETICS; RADIORECEPTOR ASSAY; RECEPTORS; NERVE CELLS; ALKYLATION; BRAIN; CELL MEMBRANES; CHICKENS; CHROMATOGRAPHY; CONCANAVALIN; EXPERIMENTAL DATA; GANGLIONS; IMMUNE SERUMS; LIGANDS; MONOCLONAL ANTIBODIES; NICOTINE; ORGANIC BROMINE COMPOUNDS; PURIFICATION; TRACER TECHNIQUES; TRITIUM COMPOUNDS; AGGLUTININS; ALKALOIDS; AMINES; AMMONIUM COMPOUNDS; ANIMAL CELLS; ANIMALS; ANTIBODIES; AUTONOMIC NERVOUS SYSTEM AGENTS; AZINES; AZOLES; BIRDS; BODY; CELL CONSTITUENTS; CENTRAL NERVOUS SYSTEM; CHEMICAL REACTIONS; DATA; DRUGS; ESTERS; FOWL; HEMAGGLUTININS; HETEROCYCLIC COMPOUNDS; INFORMATION; ISOTOPE APPLICATIONS; KINETICS; LABELLED COMPOUNDS; LECTINS; MEMBRANE PROTEINS; MEMBRANES; NERVOUS SYSTEM; NEUROREGULATORS; NUMERICAL DATA; ORGANIC COMPOUNDS; ORGANIC HALOGEN COMPOUNDS; ORGANIC NITROGEN COMPOUNDS; ORGANS; PARASYMPATHOLYTICS; PARASYMPATHOMIMETICS; PROTEINS; PYRIDINES; PYRROLES; PYRROLIDINES; QUATERNARY COMPOUNDS; REACTION KINETICS; SEPARATION PROCESSES; SOMATIC CELLS; VERTEBRATES; 550201* - Biochemistry- Tracer Techniques

Citation Formats

Stollberg, J. Characterization of a putative acetylcholine receptor in chick ciliary ganglion neurons. United States: N. p., 1985. Web.
Stollberg, J. Characterization of a putative acetylcholine receptor in chick ciliary ganglion neurons. United States.
Stollberg, J. Tue . "Characterization of a putative acetylcholine receptor in chick ciliary ganglion neurons". United States.
@article{osti_5219891,
title = {Characterization of a putative acetylcholine receptor in chick ciliary ganglion neurons},
author = {Stollberg, J},
abstractNote = {Monoclonal antibodies to the main immunogenic region on the alpha subunit of acetylcholine receptors in muscle and electric organ recognize membrane components in chick brain and ciliary ganglia that are candidates for the neuronal receptor. The component in chick brain has been purified by immunoaffinity chromatography. It specifically binds nicotine but not alpha-bungarotoxin, and can be affinity labeled with (/sup 3/H)bromoacetylcholine. The cross-reacting component in ciliary ganglion neurons is concentrated in synaptic membrane, and can be modulated by exposure of the cells to cholinergic ligands in culture. The cross-reacting component in ciliary ganglion neurons is an integral membrane component that binds concanavalin A, and it is distinct from the alpha-bungarotoxin binding component. The acetylcholine receptor function in these neurons can be locked by affinity alkylation with bromoacetylcholine, indicating similarity in this respect to receptors from muscle and electric organ. Antisera raised against the partially purified component from chick brain also block receptor function on ciliary ganglion neurons. The subcellular distribution of the ganglion component in culture is assessed, and it is shown that approximately 2/3 of the cross-reacting components are intracellular; the majority of these seem not to be destined for insertion into the plasma membrane.},
doi = {},
url = {https://www.osti.gov/biblio/5219891}, journal = {},
number = ,
volume = ,
place = {United States},
year = {1985},
month = {1}
}

Thesis/Dissertation:
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