Biochemical characterization of two nicotinic receptors from the optic lobe of the chick.
作者： M Schneider , C Adee , H Betz , J Schmidt
DOI: 10.1016/S0021-9258(17)38598-8
关键词: Nicotinic agonist 、 Ganglion type nicotinic receptor 、 Acetylcholine receptor 、 Acetylcholine binding 、 Biochemistry 、 Nicotinic Antagonist 、 Chemistry 、 Muscarinic acetylcholine receptor M5 、 Acetylcholine 、 Alpha-4 beta-2 nicotinic receptor
摘要: We have studied putative nicotinic acetylcholine receptors in the optic lobe of newborn chick, using 125I-labeled alpha-bungarotoxin, a specific blocker neuromuscular junction, and [3H]acetylcholine, ligand which presence atropine selectively labels binding sites character rat brain cortex (Schwartz et al., 1982). [3H]Acetylcholine binds reversibly to single class high affinity (KD = 2.2 X 10(-8) M) occur at tissue concentration 5.7 pmol/g. A large fraction (approximately 60%) these is solubilized by Triton X-100, sodium cholate, or zwitterionic detergent 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate. Solubilization increases for several drugs from 1.5- 7-fold. The acetylcholine-binding macromolecule resembles receptor alpha-bungarotoxin present same with respect subcellular distribution, hydrodynamic properties, lectin binding, agonist rank order. It differs toxin antagonists, sensitivity thermal inactivation, regional distribution. [3H]acetylcholine activity separated incubation agarose-linked acetylcholine, chromatography on immobilized Naja naja siamensis alpha-toxin, precipitation monoclonal antibody chick receptor.
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