A modified nicotinic acetylcholine receptor lacking the 'ion channel amphipathic helices'.

Abstract:

:Antibodies to a synthetic peptide from the 'amphipathic helix' of the alpha-chain of the nicotinic acetylcholine receptor (nAChR) bound both to detergent-solubilised and membrane-bound nAChR, indicating that this region, suggested as a component of the transmembrane ion channel in one model, is not buried in the membrane. Trypsinisation of membranes prior to affinity purification yielded preparations lacking the amphipathic helices of the alpha- and beta-chains and probably also of the gamma- and delta-chains. Such material should allow direct testing, by reconstitution experiments, of the importance of these regions for channel activity.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Roth B,Schwendimann B,Hughes GJ,Tzartos SJ,Barkas T

doi

10.1016/0014-5793(87)80374-5

subject

Has Abstract

pub_date

1987-08-31 00:00:00

pages

172-8

issue

1

eissn

0014-5793

issn

1873-3468

pii

0014-5793(87)80374-5

journal_volume

221

pub_type

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