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- W2060186952 abstract "1. 1. After the binding of [ 3 H]atropine to the circular smooth muscle layer of the bovine intestine most of the radioactivity was extracted with chloroform methanol (2:1, v/v) and after column chromatography in Sephadex LH20 the radioactivity appeared associated with a special fraction of hydrophobic protein ( i.e. Peak 3) out of five peaks obtained from the same tissue. 2. 2. This protein peak, when added to the organic extract, bound [ 3 H]atropine and [ 14 C]acetylcholine but not (+)-[ 14 C]tubocurarine. In double labelling experiments [ 3 H]atropine appeared bound to Peak 3 and [ 14 C]serotonin to another peak of hydrophobic protein ( i.e. Peak 2). 3. 3. Preliminary auto- and cross-protection experiments using unlabelled atropine (to protect the muscarinic receptor) and Dibenamine were carried out to further study the specificity of the binding. The autoprotection experiments confirmed the results of [ 3 H]atropine binding. Its control showed that 5·10 −6 M Dibenamine blocked about 85% of the binding of [ 3 H]atropine to peak 3. Cross-protection experiments using [ 14 C]serotonin or [ 14 C]histamine as ligands showed no radioactivity associated with any protein peak. 4. 4. The results obtained suggest that Peak 3 of hydrophobic protein represents a fraction containing cholinergic receptors of the muscarinic type and that this is different from the serotonin and histamine receptor. This interpretation is also supported by some quantitative considerations of our findings." @default.
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- W2060186952 date "1973-02-01" @default.
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- W2060186952 title "Receptor hydrophobic protein fraction from intestinal smooth muscle binding muscarinic ligands" @default.
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- W2060186952 doi "https://doi.org/10.1016/0005-2795(73)90049-4" @default.
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