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PROPERTIES OF A PUTATIVE MUSCARINIC CHOLTNERGIC RECEPTOR FROM DROSOPHILA MELANOGASTER
Author(s) -
Haim N.,
Nahum S.,
Dudai Y.
Publication year - 1979
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1979.tb00382.x
Subject(s) - quinuclidinyl benzilate , muscarinic acetylcholine receptor , drosophila melanogaster , muscarinic antagonist , dissociation constant , muscarinic acetylcholine receptor m1 , chemistry , acetylcholine receptor , muscarinic acetylcholine receptor m5 , muscarinic acetylcholine receptor m2 , receptor , acetylcholinesterase , biochemistry , binding site , microbiology and biotechnology , muscarinic acetylcholine receptor m3 , biology , gene , enzyme
— The powerful muscarinic antagonist [ 3 H]quinuclidinyl benzilate (QNB) specifically binds to homogenates of Drosophila melanogaster head at a level of 65 ± 6 fmol/mg protein, with an apparent dissociation constant of 0.15–0.7 nM. The half‐life of the ligand‐receptor complex at 25°C is 30–40 min. Binding is inhibited by low concentrations of muscarinic ligands but not by low concentrations of nicotinic ligands, anticholinesterases or non‐cholinergic drugs. Binding‐sites are membrane bound and are inactivated by trypsin and by Triton X‐100. Part of the activity (<20%) is released into a high speed supernatant by 2 M‐NaCI. The gene coding for the putative muscarinic receptor in Drosophila is apparently not located adjacent to the gene for acetylcholinesterase