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• W190820190 abstract "Research Article1 September 1988free access Neuronal acetylcholine receptors in Drosophila: the ARD protein is a component of a high-affinity alpha-bungarotoxin binding complex. P. Schloss P. Schloss ZMBH, Universität Heidelberg, FRG. Search for more papers by this author I. Hermans-Borgmeyer I. Hermans-Borgmeyer ZMBH, Universität Heidelberg, FRG. Search for more papers by this author H. Betz H. Betz ZMBH, Universität Heidelberg, FRG. Search for more papers by this author E. D. Gundelfinger E. D. Gundelfinger ZMBH, Universität Heidelberg, FRG. Search for more papers by this author P. Schloss P. Schloss ZMBH, Universität Heidelberg, FRG. Search for more papers by this author I. Hermans-Borgmeyer I. Hermans-Borgmeyer ZMBH, Universität Heidelberg, FRG. Search for more papers by this author H. Betz H. Betz ZMBH, Universität Heidelberg, FRG. Search for more papers by this author E. D. Gundelfinger E. D. Gundelfinger ZMBH, Universität Heidelberg, FRG. Search for more papers by this author Author Information P. Schloss1, I. Hermans-Borgmeyer1, H. Betz1 and E. D. Gundelfinger1 1ZMBH, Universität Heidelberg, FRG. The EMBO Journal (1988)7:2889-2894https://doi.org/10.1002/j.1460-2075.1988.tb03146.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info The ard gene of Drosophila melanogaster encodes a structural homologue of vertebrate nicotinic acetylcholine receptors (AChR) and is expressed exclusively in nervous tissue. To study the nature of the ARD protein, antibodies were raised against fusion constructs containing two regions of this polypeptide. One segment is putatively extracellular (amino acids 65-212), the other domain is exposed to the cytoplasm (amino acids 305-444). The ARD antisera obtained served to investigate the physical relationship between the ARD protein and alpha-bungarotoxin (alpha-Btx) binding sites occurring in Drosophila. Two different high-affinity binding sites for [125I]alpha-Btx, a highly potent antagonist of vertebrate muscle AChR, were detected in fly head membranes. Equilibrium binding and kinetic studies revealed Kd values of approximately 0.1 nM (site 1) and approximately 4 nM (site 2). The estimated maximal binding (Bmax) was approximately 240 and 1080 fmol/mg protein respectively. Both sites exhibited a nicotinic-cholinergic pharmacology. Immunoprecipitation experiments with the ARD antisera indicated that the ARD protein is associated with the [125I]alpha-Btx binding site 1 only. These data support the previously postulated hypothesis that the ARD protein is part of an alpha-Btx binding neuronal AChR of Drosophila. Furthermore, they indicate heterogeneity in nicotinic-cholinergic binding sites in the insect nervous system. Previous ArticleNext Article Volume 7Issue 91 September 1988In this issue RelatedDetailsLoading ..." @default.
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• W190820190 title "Neuronal acetylcholine receptors in Drosophila: the ARD protein is a component of a high-affinity alpha-bungarotoxin binding complex." @default.
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