(1-Pyrene)sulfonyl azide: a fluorescent probe for measuring the transmembrane topology of acetylcholine receptor subunits |
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| Authors: | J Clarke J C Garcia-Borron M Martinez-Carrion |
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| Affiliation: | 1. Division of Molecular Biology, School of Basic Life Sciences, University of Missouri, Kansas City, Missouri 64110, U.S.A.;2. Department of Biochemistry, Virginia, Commonwealth University, Richmond, Virginia 23298 U.S.A.;1. Razi University, Department of Organic Chemistry, Kermanshah, 67149-67346, Iran;2. Nanoscience & Nanotechnology Research Center (NNRC), Razi University, Kermanshah, 67149-67346, Iran;1. Department of Analytical Chemistry, Faculty of Chemistry, University College of Science, University of Tehran, P.O. Box 14155-6455, Tehran, Iran;2. Department of Applied Chemistry, Faculty of Science, University of Mohaghegh Ardabili, Iran;1. Department of Materials Engineering, Ben-Gurion University of the Negev, Beer-Sheva, Israel;2. Department of Chemistry, Ben-Gurion University of the Negev, Beer-Sheva, Israel |
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| Abstract: | (1-Pyrene)sulfonyl azide (PySA), a fluorescent, lipophilic photolabel, was used as a probe for the transmembrane topology of the acetylcholine receptor (AchR) subunits. Photolabeling of native, alkaline-extracted, and reconstituted AchR membrane preparations resulted in the labeling of all the AchR subunits. However the reconstituted AchR membrane preparations incorporated twice as much PySA into each mole of the AchR complex. Photolabeling of all subunits of the AchR does not appear to alter the agonist concentration response of AchR-mediated cation translocation. |
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