Evidence for allosteric inhibition sites in the glucose carrier of erythrocytes |
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| Affiliation: | 1. Research Institute, Agriculture Canada, University sub Post Office, London, Ontario N6A 5B7 Canada;2. Department of Biochemistry, University of Western Ontario, London, Ontario N6A 5C1 Canada;1. Department of Chemistry, Rice University, 6100 Main Street, Houston, TX, 77005, USA;2. Université Laval, Département de Chimie, Pavillon Alexandre-Vachon Bureau 1407, Quebec City, 4137, Canada;3. Smalley Institute for Nanoscale Science and Technology, Rice University, 6100 Main Street, Houston, TX, 77005, USA;4. Department of Materials Science and NanoEngineering, Rice University, 6100 Main Street, Houston, TX 77005, USA;1. Department of Pharmaceutical Care and Health Sciences, Faculty of Pharmaceutical Sciences, Fukuoka University, Fukuoka, Japan;2. BBB Laboratory, PharmaCo-Cell Co., Ltd., Nagasaki, Japan;1. Department of Physics of Polymers and Crystals, Faculty of Physics, M.V. Lomonosov Moscow State University, Leninskie Gory 1, 119991, Moscow, Russia;2. A.N. Nesmeyanov Institute of Organoelement Compounds of Russian Academy of Sciences, Vavilova St. 28, INEOS, 119991, Moscow, Russia;3. Institute of Advanced Energy-Related Nanomaterials, University of Ulm, Albert-Einstein-Allee 11, D-89069, Ulm, Germany;4. D.I. Mendeleev University of Chemical Technology of Russia, Moscow, Russia;1. College of Physics, University-Industry Joint Center for Ocean Observation and Broadband Communication, Qingdao University, Qingdao 266071, China;2. National Demonstration Center for Experiment Applied Physics Education (Qingdao University), Qingdao 266071, China;3. Shandong Provincial University Key Laboratory of Optoelectrical Material Physics and Devices, Qingdao 266071, China |
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| Abstract: | 2,4-Fluorodinitrobenzene and 2,3-butanedione, which irreversibly inactivate the glucose transfer system of erythrocytes, have been used as probes to determine whether the substrate site and inner and outer sites for reversible inhibitors are located in the same or different regions of the carrier. Inhibitors bound at an inhibition site exposed in the inward-facing but not the outwardfacing form of the carrier (cytochalasin B, androstendione and androstandione) protect the transport system against inactivation by 2,4-fluorodinitrobenzene. Inhibitors bound at an external inhibition site (phloretin) and substrates bound at the transfer site do not protect. In contrast inactivation by 2,3-butanedione is slightly accelerated by internally bound inhibitors, while substrates and substrate analogs bound at the transfer site protect the system. It is shown that fluorodinitrobenzene reacts in the inner inhibition site and butanedione in the substrate site; and further that these sites may be separate binding areas in the carrier linked by allosteric interaction. The consequence of this linkage is that binding of a ligand at the substrate site precludes binding of another ligand at the internal or external inhibition site. |
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