Abstract
Restriction fragments of DNA derived from a cDNA clone of the alpha subunit of the acetylcholine receptor were subcloned in Escherichia coli by using the trpE fusion vector, pATH2. Transformants expressing the amino acid sequences 166-315 or 166-200 are shown to produce a chimeric protein that bound alpha-bungarotoxin. Moreover, it is shown that sufficient amounts of toxin-binding proteins can be generated by individual colonies of bacteria. This provides a new approach for gene selection via functional expression--i.e., ligand overlays of colony blots.
MeSH Terms
Animals
Bungarotoxins/metabolism
Cloning, Molecular
DNA/metabolism
Escherichia coli/genetics
Genes
Genetic Vectors
Plasmids
Receptors, Cholinergic/genetics
Receptors, Nicotinic/genetics
Torpedo
alpha7 Nicotinic Acetylcholine Receptor
Chemicals
Bungarotoxins
Receptors, Cholinergic
Receptors, Nicotinic
alpha7 Nicotinic Acetylcholine Receptor
DNA
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Gershoni J M
References (18)
18 references, click to expand
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