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Monoclonal antibodies raised to the 190\u2013203 synthetic fragment of rabies virus glycoprotein were immobilized on a high performance affinity chromatography column and were able to bind neurotoxins. Toxins were displaced from the affinity column by elution at acidic pH and by affinity competition with acetylcholine at neutral pH. Furthermore, the affinity column proved to be useful for the purification of cholinergic ligands. Overall, these results indicate that the paratope of our monoclonal antibodies could behave as an \u2018internal image\u2019 of the nicotinic cholinergic receptor acetylcholine binding site.<\/jats:p>","DOI":"10.1002\/jmr.300020202","type":"journal-article","created":{"date-parts":[[2005,5,29]],"date-time":"2005-05-29T10:25:55Z","timestamp":1117362355000},"page":"51-55","source":"Crossref","is-referenced-by-count":11,"title":["A monoclonal antibody to a synthetic fragment of rabies virus glycoprotein binds ligands of the nicotinic cholinergic receptor"],"prefix":"10.1002","volume":"2","author":[{"given":"Mauro","family":"Rustici","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Annalisa","family":"Santucci","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Luisa","family":"Lozzi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Simonetta","family":"Petreni","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Adriano","family":"Spreafico","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Paolo","family":"Neri","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Luisa","family":"Bracci","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Patrizia","family":"Soldani","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2004,2,3]]},"reference":[{"key":"e_1_2_1_2_1","doi-asserted-by":"publisher","DOI":"10.1016\/0161-5890(88)90125-3"},{"key":"e_1_2_1_3_1","doi-asserted-by":"publisher","DOI":"10.1016\/0003-2697(81)90281-5"},{"key":"e_1_2_1_4_1","doi-asserted-by":"publisher","DOI":"10.1089\/hyb.1983.2.451"},{"key":"e_1_2_1_5_1","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.bi.51.070182.002423"},{"key":"e_1_2_1_6_1","doi-asserted-by":"publisher","DOI":"10.1056\/NEJM198209233071301"},{"key":"e_1_2_1_7_1","doi-asserted-by":"publisher","DOI":"10.3109\/10409238309102792"},{"key":"e_1_2_1_8_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi00350a019"},{"key":"e_1_2_1_9_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.80.13.4089"},{"key":"e_1_2_1_10_1","first-page":"14","volume-title":"Gel Electrophoresis of Proteins","author":"Hames B. 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