Properties of the nicotinic acetylcholine receptor macromolecule ofElectrophorus electricus
نویسندگان
چکیده
منابع مشابه
Subunit structure of the acetylcholine receptor from Electrophorus electricus.
The amino-terminal amino acid sequences of the four major peptides (Mr 41,000, 50,000, 55,000, and 62,000) present in purified preparations of Electrophorus electricus nicotinic acetylcholine receptor (AcChoR) have been determined for 24 cycles by automated sequence analysis procedures yielding four unique polypeptide sequences. The sequences showed a high degree of similarity, having identical...
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The properties of the channel of the purified acetylcholine receptor (AChR) were investigated after reconstitution in planar lipid bilayers . The time course of the agonist-induced conductance exhibits a transient peak that relaxes to a steady state value. The macroscopic steady state membrane conductance increases with agonist concentration, reaching saturation at 10-5 M for carbamylcholine (C...
متن کاملPurification and characterization of acetylcholine receptor-I from Electrophorus electricus.
A Triton X-100 extract of electric tissue was subjected to a single step affinity chromatography using either of two affinity gels: [N-(6-aminocaproyl)-p-aminobenzyl]trimethylammonium bromide or methyl[(6-aminocaproyl-6'-aminocaproyl)-3-amino]pyridinium bromide attached to Sepharose 4B. Specific elution of the acetylcholine receptor-I (AcChR-I) with low concentration of a bis-quaternary agonist...
متن کاملConformation of acetylcholine bound to the nicotinic acetylcholine receptor.
We report here the biologically active conformation of acetylcholine when bound to the high-affinity state of the receptor from Torpedo californica. The acetylcholine conformation was determined in the free and bound states by proton NMR two-dimensional nuclear Overhauser effects. In agreement with x-ray crystallographic data, acetylcholine in solution has an extended conformation with an avera...
متن کاملEmbedded cholesterol in the nicotinic acetylcholine receptor.
The nicotinic acetylcholine receptor (nAChR) is a cation-selective channel central to both neuronal and muscular processes and is considered the prototype for ligand-gated ion channels, motivating a structural determination effort that spanned several decades [Unwin N (2005) Refined structure of the nicotinic acetylcholine receptor at 4 A resolution. J Mol Biol 346:967-989]. Purified nAChR must...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1972
ISSN: 0014-5793
DOI: 10.1016/0014-5793(72)80382-x