Expression of the alpha-bungarotoxin binding site of the nicotinic acetylcholine receptor by Escherichia coli transformants.
- 1 June 1987
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 84 (12) , 4318-4321
- https://doi.org/10.1073/pnas.84.12.4318
Abstract
Restriction fragments of DNA derived from 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 acids 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 provide a new approach for gene selection via functional expression-i.e, ligand overlays of colony blots.This publication has 20 references indexed in Scilit:
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